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3RCK

Human Cyclophilin D Complexed with a Fragment

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 Residues10
DetailsBINDING SITE FOR RESIDUE 1FP X 208
ChainResidue
XGLY114
XHOH297
XTHR115
XASN144
XTHR149
XGLN153
X1FP209
XHOH239
XHOH240
XHOH284

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 1FP X 209
ChainResidue
XHIS96
XARG97
XGLN105
XGLY114
XASN144
XGLN153
X1FP208
X1FP210
XHOH281
XHOH298
XHOH377

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 1FP X 210
ChainResidue
XPHE102
XMET103
XGLN105
XALA143
XASN144
XLEU164
XHIS168
X1FP209
XHOH315
XHOH403

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 1FP X 211
ChainResidue
XGLY56
XILE99
XSER101
XPHE102
XILE159
XLYS197
XHOH345

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 1FP X 212
ChainResidue
XASN45
XLYS67
XASP69
XASN111
XTHR115
XHOH243
XHOH244
XHOH245
XHOH246
XHOH354

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

219869

PDB entries from 2024-05-15

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