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5CCN

Human Cyclophilin D Complexed with 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 Residues2
Detailsbinding site for residue K A 201
ChainResidue
APGE204
APGE204

site_idAC2
Number of Residues7
Detailsbinding site for residue FMT A 202
ChainResidue
ACYS40
ATHR41
ALYS49
ACYS161
AHOH322
AHOH334
AHOH374

site_idAC3
Number of Residues4
Detailsbinding site for residue PG4 A 203
ChainResidue
AVAL93
APRO95
AHIS131
AHOH375

site_idAC4
Number of Residues6
Detailsbinding site for residue PGE A 204
ChainResidue
APRO58
ASER59
ATRP121
ALYS148
AK201
AK201

site_idAC5
Number of Residues2
Detailsbinding site for residue PEG A 205
ChainResidue
AGLN163
ASER165

site_idAC6
Number of Residues11
Detailsbinding site for residue 4ZZ A 206
ChainResidue
AARG55
AGLN63
AGLY72
ATHR73
AALA101
AASN102
ATHR107
AGLN111
APHE113
AHIS126
AHOH405

Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgStFHRVIpsFMcQAG
ChainResidueDetails
ATYR48-GLY65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS25

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS44
AILE133
ALYS148

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS125

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ACYS161

225399

PDB entries from 2024-09-25

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