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1RHU

CRYSTAL STRUCTURE OF THE COMPLEX OF CASPASE-3 WITH A 5,6,7 TRICYCLIC PEPTIDOMIMETIC INHIBITOR

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 Residues18
DetailsBINDING SITE FOR RESIDUE 3CY A 501
ChainResidue
AHOH16
BSER339
BTRP340
BARG341
BASN342
BSER343
BTRP348
BSER381
BPHE381
BPHE381
AHOH47
AHOH55
AARG179
AHIS237
AGLU239
AGLN283
ACYS285
ATHR288

Functional Information from PROSITE/UniProt
site_idPS01121
Number of Residues15
DetailsCASPASE_HIS Caspase family histidine active site. HskrsSfvCvLLSHG
ChainResidueDetails
AHIS224-GLY238

site_idPS01122
Number of Residues12
DetailsCASPASE_CYS Caspase family cysteine active site. KPKLFIIQACRG
ChainResidueDetails
ALYS276-GLY287

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120, ECO:0000269|PubMed:36423631
ChainResidueDetails
BARG341
ACYS285

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine; in inhibited form => ECO:0000269|PubMed:10213689
ChainResidueDetails
ACYS285

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1qx3
ChainResidueDetails
ACYS285
AHIS237
AGLY238

site_idMCSA1
Number of Residues
DetailsM-CSA 815
ChainResidueDetails
ATHR177electrostatic stabiliser
ASER178electrostatic stabiliser
AHIS237electrostatic stabiliser, proton acceptor, proton donor
AGLY238electrostatic stabiliser
ACYS285electrostatic stabiliser

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PDB entries from 2024-09-11

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