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3RCI

Human cyclophilin D complexed with 5-methyl-1,2-oxazol-3-amine

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 Residues6
DetailsBINDING SITE FOR RESIDUE M3I X 1
ChainResidue
XARG97
XALA143
XASN144
XHIS168
XM3I208
XHOH228

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE M3I X 208
ChainResidue
XGLN105
XASN113
XGLY114
XTHR131
XM3I209
XM3I1
XHIS96
XARG97

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE M3I X 209
ChainResidue
XGLN105
XGLY114
XARG124
XALA143
XASN144
XTHR149
XGLN153
XM3I208
XHOH339
XHOH361
XHOH449

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE M3I X 210
ChainResidue
XVAL135
XGLY136
XPRO137
XHIS173
XHOH300
XHOH301

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

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PDB entries from 2024-11-06

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