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

4J5A

Human Cyclophilin D Complexed with an Inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
X0000413biological_processprotein peptidyl-prolyl isomerization
X0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
X0006457biological_processprotein folding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 67Z X 301
ChainResidue
XARG97
XGLY151
XGLN153
XPHE155
XLEU164
XHIS168
XHOH469
XHOH486
XHOH525
XPHE102
XMET103
XGLN105
XGLY114
XARG124
XALA143
XASN144
XTHR149

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE DMS X 302
ChainResidue
XVAL174
XILE175
XGLU176
XGLY177
XMET178

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgStFHRVIpsFMcQAG
ChainResidueDetails
XTYR90-GLY107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
XLYS67

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
XLYS86
XILE175
XLYS190

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
XLYS167

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
XCYS203

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon