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5A0E

Crystal structure of cyclophilin D in complex with CsA analogue, JW47.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
B0000413biological_processprotein peptidyl-prolyl isomerization
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0006457biological_processprotein folding
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 Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS25
BLYS25

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS44
AILE133
ALYS148
BLYS44
BILE133
BLYS148

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ALYS125
BLYS125

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q99KR7
ChainResidueDetails
ACYS161
BCYS161

219869

PDB entries from 2024-05-15

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