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3RCL

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 Residues12
DetailsBINDING SITE FOR RESIDUE 5AO A 1
ChainResidue
AASP69
AHOH247
AHOH522
AHOH523
AVAL70
AGLY114
ATHR115
AARG124
AASN144
ATHR149
AGLY151
AGLN153

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE P4C A 208
ChainResidue
AILE120
AVAL135
AGLY136
APRO137
AHIS173
AHOH400
AHOH450
AHOH481
AHOH515
AHOH528

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 Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS67

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS86
AILE175
ALYS190

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS167

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ACYS203

224572

PDB entries from 2024-09-04

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