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5TRC

Crystal structure of phosphorylated AC3-AC5 domains of yeast acetyl-CoA carboxylase

Functional Information from GO Data
ChainGOidnamespacecontents
A0003989molecular_functionacetyl-CoA carboxylase activity
A0005524molecular_functionATP binding
A0006633biological_processfatty acid biosynthetic process
B0003989molecular_functionacetyl-CoA carboxylase activity
B0005524molecular_functionATP binding
B0006633biological_processfatty acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL A 1601
ChainResidue
AVAL1082
APHE1083
AARG1108

site_idAC2
Number of Residues3
Detailsbinding site for residue CL B 1601
ChainResidue
BPHE1083
BARG1108
BTYR1272

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER1148
BSER1148

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASEP1157
BSEP1157

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER1162
BSER1162

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PDB entries from 2024-05-01

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