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1Y0O

crystal structure of reduced AtFKBP13

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0009507cellular_componentchloroplast
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0009507cellular_componentchloroplast
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0009507cellular_componentchloroplast
D0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
D0009507cellular_componentchloroplast
E0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
E0009507cellular_componentchloroplast
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues495
DetailsDomain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
AASP48
ATYR99
AILE67

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
BASP248
BTYR299
BILE267

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
CILE467
CTYR499
CASP448

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
DASP648
DILE667
DTYR699

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1d6o
ChainResidueDetails
EILE867
ETYR899
EASP848

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PDB entries from 2026-01-28

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