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5R43

Crystal Structure of deuterated gamma-Chymotrypsin at pH 7.5, cryo temperature

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 Residues12
Detailsbinding site for residue MLA A 101
ChainResidue
ACYS1
BLYS93
BHOH328
BHOH332
AGLY2
AVAL3
AHOH201
AHOH202
AHOH203
AHOH205
AHOH212
BTHR37

site_idAC2
Number of Residues2
Detailsbinding site for residue IOD B 201
ChainResidue
BHOH440
BHOH440

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_idMCSA1
Number of Residues3
DetailsM-CSA 387
ChainResidueDetails
CGLY193electrostatic stabiliser
CSER195covalent catalysis
CGLY196electrostatic stabiliser

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PDB entries from 2024-06-26

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