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1CHO

CRYSTAL AND MOLECULAR STRUCTURES OF THE COMPLEX OF ALPHA-*CHYMOTRYPSIN WITH ITS INHIBITOR TURKEY OVOMUCOID THIRD DOMAIN AT 1.8 ANGSTROMS RESOLUTION

Functional Information from GO Data
ChainGOidnamespacecontents
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
G0004252molecular_functionserine-type endopeptidase activity
G0006508biological_processproteolysis
I0004867molecular_functionserine-type endopeptidase inhibitor activity
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
FVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SScmGDSGGPLV
ChainResidueDetails
GSER189-VAL200

site_idPS00282
Number of Residues23
DetailsKAZAL_1 Kazal serine protease inhibitors family signature. CtleyRplCgSdnktYgnkCnf.C
ChainResidueDetails
ICYS16-CYS38

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Reactive bond 3 for chymotrypsin, elastase, proteases A and B, and subtilisin
ChainResidueDetails
ILEU18
FASP102

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
IASN45

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hja
ChainResidueDetails
GSER195
GGLY193

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hja
ChainResidueDetails
FASP102
FHIS57
GSER195
GGLY196

site_idMCSA1
Number of Residues3
DetailsM-CSA 387
ChainResidueDetails
GGLY193electrostatic stabiliser
GSER195covalent catalysis
GGLY196electrostatic stabiliser

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PDB entries from 2024-07-31

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