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1Q6U

Crystal structure of FkpA from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0006457biological_processprotein folding
A0016853molecular_functionisomerase activity
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042026biological_processprotein refolding
A0042597cellular_componentperiplasmic space
A0044183molecular_functionprotein folding chaperone
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CS A 246
ChainResidue
ASER66
AALA111
AGLU113
AVAL116

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues85
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
ATYR200
AILE174
AASP157

247947

PDB entries from 2026-01-21

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