DB code: D00224

RLCP classification 1.13.30000.10 : Hydrolysis
CATH domain 2.40.10.10 : Thrombin, subunit H Catalytic domain
2.40.10.10 : Thrombin, subunit H Catalytic domain
E.C. 3.4.21.81
CSA 1ds2
M-CSA 1ds2
MACiE

CATH domain Related DB codes (homologues)
2.40.10.10 : Thrombin, subunit H M00139 D00214 M00167 D00426 M00133 D00428 D00429 D00430 D00431 D00432 D00433 D00434 D00435 M00227 M00209 D00194 D00197 D00211 D00212 D00216 M00212 D00497 M00217 M00216 D00528 D00848 D00850 D00851 D00852 D00855 M00152 M00155 M00157 M00181 M00315 M00316 M00317 M00348 M00349 T00074 T00410 T00411

Uniprot Enzyme Name
UniprotKB Protein name Synonyms MEROPS Pfam
P00777 Streptogrisin-B
EC 3.4.21.81
Pronase enzyme B
SGPB
Serine protease B
S01.262 (Serine)
PF02983 (Pro_Al_protease)
PF00089 (Trypsin)
[Graphical View]

KEGG enzyme name
streptogrisin B
Streptomyces griseus protease B
pronase B
serine proteinase B
Streptomyces griseus proteinase B
Streptomyces griseus proteinase 1
Streptomyces griseus serine proteinase B

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00777 PRTB_STRGR Hydrolysis of proteins with trypsin-like specificity. Monomer.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C00017 C00012 C00001 C00017 C00012 I00087 I00085 I00086
E.C.
Compound Protein Peptide H2O Protein Peptide Peptidyl-tetrahedral intermediate Acyl-enzyme Tetrahedral intermediate
Type peptide/protein peptide/protein H2O peptide/protein peptide/protein
ChEBI 15377
PubChem 22247451
962
1csoE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ct0E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ct2E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ct4E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ds2E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1sgdE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1sgeE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1sgnE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1sgpE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1sgqE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1sgrE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1sgyE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2sgdE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2sgeE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2sgfE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2sgpE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2sgqE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3sgbE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3sgqE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
4sgbE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1csoE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ILE_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1ct0E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:SER_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1ct2E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:THR_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1ct4E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:VAL_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1ds2E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:1LU_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1sgdE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ASP_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1sgeE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GLU_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1sgnE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ASN_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1sgpE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ALA_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1sgqE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GLY_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1sgrE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:LEU_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
1sgyE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:TYR_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
2sgdE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:ASP_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
2sgeE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GLU_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
2sgfE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PHE_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
2sgpE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:PRO_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
2sgqE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GLN_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
3sgbE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:LEU_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
3sgqE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:GLN_18-GLU_19(chain I) Unbound Unbound Unbound Unbound Unbound
4sgbE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:LEU_38-ASN_39(chain I) Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
PDB;1sgd, 1sge, 1sgn, 1sgp,1sgq,1sgr, 2sgd, 2sge, 2sgf, 2sgp, 2sgq, 3sgq & Swiss-prot;P00777 & literature [3], [5], [7]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1csoE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1ct0E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1ct2E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1ct4E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1ds2E01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1sgdE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1sgeE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1sgnE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1sgpE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1sgqE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1sgrE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1sgyE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
2sgdE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
2sgeE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
2sgfE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
2sgpE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
2sgqE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
3sgbE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
3sgqE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
4sgbE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain HIS 57;ASP 102
1csoE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1ct0E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1ct2E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1ct4E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1ds2E02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1sgdE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1sgeE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1sgnE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1sgpE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1sgqE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1sgrE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
1sgyE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
2sgdE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
2sgeE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
2sgfE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
2sgpE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
2sgqE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
3sgbE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
3sgqE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195
4sgbE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain SER 195 GLY 193;SER 195

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[5]
p.142
[7]
p.431
[9]

References
[1]
Resource
Comments ACTIVE SITE.
Medline ID 68124983
PubMed ID 5636372
Journal Biochim Biophys Acta
Year 1968
Volume 151
Pages 402-8
Authors Wahlby S, Engstrom L
Title Studies on Streptomyces griseus protease. II. The amino acid sequence around the reactive serine residue of DFP-sensitive components with esterase activity.
Related PDB
Related UniProtKB P00777
[2]
Resource
Comments ACTIVE SITE.
Medline ID 74302902
PubMed ID 4212092
Journal FEBS Lett
Year 1974
Volume 43
Pages 81-5
Authors Gertler A
Title Inhibition of Streptomyces griseus protease B by peptide chloromethyl ketones: partial mapping of the binding site and identification of the reactive residue.
Related PDB
Related UniProtKB P00777
[3]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND REVISIONS.
Medline ID 76051298
PubMed ID 1186854
Journal Nature
Year 1975
Volume 257
Pages 758-63
Authors Delbaere LT, Hutcheon WL, James MN, Thiessen WE
Title Tertiary structural differences between microbial serine proteases and pancreatic serine enzymes.
Related PDB
Related UniProtKB P00777
[4]
Resource
Comments
Medline ID
PubMed ID 413567
Journal Biochemistry
Year 1978
Volume 17
Pages 375-80
Authors Bauer CA
Title Active centers of Streptomyces griseus protease 1, Streptomyces griseus protease 3, and alpha-chymotrypsin: enzyme-substrate interactions.
Related PDB
Related UniProtKB
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), AND REVISIONS.
Medline ID 79210651
PubMed ID 110426
Journal Can J Biochem
Year 1979
Volume 57
Pages 135-44
Authors Delbaere LT, Brayer GD, James MN
Title The 2.8 A resolution structure of Streptomyces griseus protease B and its homology with alpha-chymotrypsin and Streptomyces griseus protease A.
Related PDB
Related UniProtKB P00777
[6]
Resource
Comments
Medline ID
PubMed ID 6769571
Journal Can J Biochem
Year 1980
Volume 58
Pages 252-71
Authors James MN
Title An X-ray crystallographic approach to enzyme structure and function.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 6777499
Journal J Mol Biol
Year 1980
Volume 139
Pages 423-38
Authors James MN, Brayer GD, Delbaere LT, Sielecki AR, Gertler A
Title Crystal structure studies and inhibition kinetics of tripeptide chloromethyl ketone inhibitors with Streptomyces griseus protease B.
Related PDB
Related UniProtKB
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF THIRD DOMAIN.
Medline ID 83014993
PubMed ID 6750612
Journal Proc Natl Acad Sci U S A
Year 1982
Volume 79
Pages 4868-72
Authors Fujinaga M, Read RJ, Sielecki A, Ardelt W, Laskowski M Jr, James MN
Title Refined crystal structure of the molecular complex of Streptomyces griseus protease B, a serine protease, with the third domain of the ovomucoid inhibitor from turkey.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 6414511
Journal Biochemistry
Year 1983
Volume 22
Pages 4420-33
Authors Read RJ, Fujinaga M, Sielecki AR, James MN
Title Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-A resolution.
Related PDB 3sgb
Related UniProtKB
[10]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 55-106.
Medline ID 89178636
PubMed ID 2494344
Journal J Mol Biol
Year 1989
Volume 205
Pages 201-28
Authors Greenblatt HM, Ryan CA, James MN
Title Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 A resolution.
Related PDB 4sgb
Related UniProtKB P00777
[11]
Resource
Comments
Medline ID
PubMed ID 8495199
Journal Protein Sci
Year 1993
Volume 2
Pages 786-99
Authors Bigler TL, Lu W, Park SJ, Tashiro M, Wieczorek M, Wynn R, Laskowski M Jr
Title Binding of amino acid side chains to preformed cavities: interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 7499197
Journal J Biol Chem
Year 1995
Volume 270
Pages 27419-22
Authors Abul Qasim M, Ranjbar MR, Wynn R, Anderson S, Laskowski M Jr
Title Ionizable P1 residues in serine proteinase inhibitors undergo large pK shifts on complex formation.
Related PDB
Related UniProtKB
[13]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8535235
Journal Protein Sci
Year 1995
Volume 4
Pages 1985-97
Authors Huang K, Lu W, Anderson S, Laskowski M Jr, James MN
Title Water molecules participate in proteinase-inhibitor interactions: crystal structures of Leu18, Ala18, and Gly18 variants of turkey ovomucoid inhibitor third domain complexed with Streptomyces griseus proteinase B.
Related PDB 1sgp 1sgq 1sgr
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 9020764
Journal Biochemistry
Year 1997
Volume 36
Pages 673-9
Authors Lu W, Qasim MA, Laskowski M Jr, Kent SB
Title Probing intermolecular main chain hydrogen bonding in serine proteinase-protein inhibitor complexes: chemical synthesis of backbone-engineered turkey ovomucoid third domain.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 9878379
Journal J Mol Biol
Year 1998
Volume 284
Pages 1683-94
Authors Fujinaga M, Huang K, Bateman KS, James MN
Title Computational analysis of the binding of P1 variants of domain 3 of turkey ovomucoid inhibitor to Streptomyces griseus protease B.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 10712933
Journal Chem Biol
Year 2000
Volume 7
Pages 163-71
Authors Elliott RJ, Bennet AJ, Braun CA, MacLeod AM, Borgford TJ
Title Active-site variants of Streptomyces griseus protease B with peptide-ligation activity.
Related PDB
Related UniProtKB
[17]
Resource
Comments X-RAY DIFFRACTION
Medline ID
PubMed ID 10739250
Journal Protein Sci
Year 2000
Volume 9
Pages 83-94
Authors Bateman KS, Anderson S, Lu W, Qasim MA, Laskowski M Jr, James MN
Title Deleterious effects of beta-branched residues in the S1 specificity pocket of Streptomyces griseus proteinase B (SGPB): crystal structures of the turkey ovomucoid third domain variants Ile18I, Val18I, Thr18I, and Ser18I in complex with SGPB.
Related PDB 1cso 1ct0 1ct2 1ct4
Related UniProtKB
[18]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11162096
Journal J Mol Biol
Year 2001
Volume 305
Pages 839-49
Authors Bateman KS, Huang K, Anderson S, Lu W, Qasim MA, Laskowski M Jr, James MN
Title Contribution of peptide bonds to inhibitor-protease binding: crystal structures of the turkey ovomucoid third domain backbone variants OMTKY3-Pro18I and OMTKY3-psi[COO]-Leu18I in complex with Streptomyces griseus proteinase B (SGPB) and the structure of the free inhibitor, OMTKY-3-psi[CH2NH2+]-Asp19I.
Related PDB 1ds2 2sgp
Related UniProtKB
[19]
Resource
Comments
Medline ID
PubMed ID 14718653
Journal Protein Sci
Year 2004
Volume 13
Pages 381-90
Authors Truhlar SM, Cunningham EL, Agard DA
Title The folding landscape of Streptomyces griseus protease B reveals the energetic costs and benefits associated with evolving kinetic stability.
Related PDB
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 15740746
Journal J Mol Biol
Year 2005
Volume 347
Pages 355-66
Authors Jaswal SS, Truhlar SM, Dill KA, Agard DA
Title Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases.
Related PDB
Related UniProtKB

Comments
This enzyme belongs to the peptidase family-S1E.
This enzyme has got a catalytic triad composed of Ser/His/Asp, it should have the same mechanism as that of trypsin (D00197 in EzCatDB).

Created Updated
2003-10-14 2011-02-21