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3RDB

Human Cyclophilin D Complexed with a Fragment

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 Residues11
DetailsBINDING SITE FOR RESIDUE P4C A 1
ChainResidue
AILE120
AHOH510
AHOH539
AVAL135
AGLY136
APRO137
AHIS173
AHOH403
AHOH430
AHOH439
AHOH458

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR RESIDUE 5MZ A 208
ChainResidue
AGLY44
AASP69
AVAL70
AGLY114
ATHR115
AARG124
AASN144
ATHR149
AGLY151
AGLN153
AHOH247
AHOH287
AHOH431
AHOH432
AHOH452

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 Residues156
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"Q99KR7","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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