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2YL2

Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0003989molecular_functionacetyl-CoA carboxylase activity
A0005524molecular_functionATP binding
A0046872molecular_functionmetal ion binding
B0003989molecular_functionacetyl-CoA carboxylase activity
B0005524molecular_functionATP binding
B0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00866
Number of Residues15
DetailsCPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMIKASeggGGkG
ChainResidueDetails
ATYR343-GLY357

site_idPS00867
Number of Residues8
DetailsCPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL
ChainResidueDetails
APHE472-LEU479

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00969","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues191
DetailsDomain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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