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4JR0

Human procaspase-3 bound to Ac-DEVD-CMK

Functional Information from GO Data
ChainGOidnamespacecontents
A0004197molecular_functioncysteine-type endopeptidase activity
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A 301
ChainResidue
ALYS53
AGLY66
ATHR67
AASP68

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL B 301
ChainResidue
BLYS53
BGLY66
BTHR67
BASP68

site_idAC3
Number of Residues22
DetailsBINDING SITE FOR CHAIN C OF AC-DEVD-CMK
ChainResidue
ASER120
AHIS121
AGLY122
AGLN161
ACYS163
ASER205
ATRP206
AARG207
AASN208
ASER209
ASER249
APHE250
AHOH447
AHOH584
AHOH612
CHOH201
CHOH202
CHOH203
CHOH204
CHOH205
CHOH206
AARG64

site_idAC4
Number of Residues22
DetailsBINDING SITE FOR CHAIN D OF AC-DEVD-CMK
ChainResidue
BARG64
BSER120
BHIS121
BGLY122
BGLN161
BCYS163
BSER205
BTRP206
BARG207
BASN208
BSER209
BTRP214
BSER249
BPHE250
BHOH460
BHOH494
BHOH568
DHOH201
DHOH202
DHOH203
DHOH204
DHOH205

Functional Information from PROSITE/UniProt
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HskrsSfvCvLLSHG
ChainResidueDetails
AHIS108-GLY122

site_idPS01122
Number of Residues12
DetailsCASPASE_CYS Caspase family cysteine active site. KPKLFIIQACRG
ChainResidueDetails
ALYS154-GLY165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P29466
ChainResidueDetails
AHIS121
ACYS163
BHIS121
BCYS163

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine; in inhibited form => ECO:0000269|PubMed:10213689
ChainResidueDetails
ACYS163
BCYS163

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:36423631
ChainResidueDetails
AARG207
BARG207

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 815
ChainResidueDetails
ATHR62electrostatic stabiliser
ASER63electrostatic stabiliser
AHIS121electrostatic stabiliser, proton acceptor, proton donor
AGLY122electrostatic stabiliser
ACYS163electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 815
ChainResidueDetails
BTHR62electrostatic stabiliser
BSER63electrostatic stabiliser
BHIS121electrostatic stabiliser, proton acceptor, proton donor
BGLY122electrostatic stabiliser
BCYS163electrostatic stabiliser

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PDB entries from 2024-05-01

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