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1GGD

CRYSTAL STRUCTURE OF GAMMA CHYMOTRYPSIN WITH N-ACETYL-LEUCIL-PHENYLALANINE ALDEHYDE BOUND AT THE ACTIVE SITE

Functional Information from GO Data
ChainGOidnamespacecontents
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
C0004252molecular_functionserine-type endopeptidase activity
C0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 401
ChainResidue
AHOH544
AHOH645
BLYS36
BSER92
BHOH560
BHOH604
CTRP237
CHOH656

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE FAF C 301
ChainResidue
CSER190
CCYS191
CMET192
CGLY193
CASP194
CSER195
CSER214
CTRP215
CGLY216
CSER217
CHOH640
CHOH711
BHIS57

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
BVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. SScmGDSGGPLV
ChainResidueDetails
CSER189-VAL200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Charge relay system
ChainResidueDetails
CSER195
BASP102

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1hja
ChainResidueDetails
CSER195
CGLY193

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1hja
ChainResidueDetails
CSER195
CGLY196
BASP102
BHIS57

site_idMCSA1
Number of Residues3
DetailsM-CSA 387
ChainResidueDetails
CGLY193electrostatic stabiliser
CSER195covalent catalysis
CGLY196electrostatic stabiliser

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PDB entries from 2024-07-10

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