Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4J58

Human Cyclophilin D Complexed with an Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 53Z A 301
ChainResidue
AARG97
AGLN153
APHE155
AHIS168
AHOH477
AHOH497
AHOH618
APHE102
AMET103
AGLN105
AGLY114
AARG124
AALA143
AASN144
ATHR149

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 302
ChainResidue
ALEU164
ALYS167
AHIS168
AHOH521
AHOH599
AHOH717
AHOH735

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgStFHRVIpsFMcQAG
ChainResidueDetails
ATYR90-GLY107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS67

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS86
AILE175
ALYS190

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS167

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ACYS203

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon