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1BDO

STRUCTURE OF THE BIOTINYL DOMAIN OF ACETYL-COENZYME A CARBOXYLASE DETERMINED BY MAD PHASING

Functional Information from GO Data
ChainGOidnamespacecontents
A0003989molecular_functionacetyl-CoA carboxylase activity
A0006633biological_processfatty acid biosynthetic process
A0009317cellular_componentacetyl-CoA carboxylase complex
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE BTN A 157
ChainResidue
ATYR92
ATHR94
APRO95
ASER96
APRO97
ALYS122
AGLU156
AHOH304
AHOH311

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

246905

PDB entries from 2025-12-31

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