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2GCH

REFINED CRYSTAL STRUCTURE OF GAMMA-CHYMOTRYPSIN AT 1.9 ANGSTROMS RESOLUTION

Replaces:  1GCH
Functional Information from GO Data
ChainGOidnamespacecontents
F0004252molecular_functionserine-type endopeptidase activity
F0006508biological_processproteolysis
G0004252molecular_functionserine-type endopeptidase activity
G0006508biological_processproteolysis
Functional Information from PDB Data
site_idBND
Number of Residues9
DetailsRESIDUES WHICH ARE INVOLVED IN THE SUBSTRATE BINDING SITE
ChainResidue
GSER218
GCYS220
GTYR228
GSER190
GCYS191
GMET192
GVAL213
GSER214
GTRP215

site_idCAT
Number of Residues3
DetailsCATALYTIC CENTER OF THE MOLECULE
ChainResidue
FHIS57
FASP102
GSER195

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Charge relay system
ChainResidueDetails
GSER195
FASP102

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 2024-07-17

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