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3BDO

SOLUTION STRUCTURE OF APO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY

Functional Information from GO Data
ChainGOidnamespacecontents
A0003989molecular_functionacetyl-CoA carboxylase activity
A0006633biological_processfatty acid biosynthetic process
A0009317cellular_componentacetyl-CoA carboxylase complex
Functional Information from PROSITE/UniProt
site_idPS00188
Number of Residues18
DetailsBIOTIN Biotin-requiring enzymes attachment site. GDtLciVeAMKMmnqIeA
ChainResidueDetails
AGLY112-ALA129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsModified residue: {"description":"N6-biotinyllysine","evidences":[{"source":"PROSITE-ProRule","id":"PRU01066","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"324999","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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