5TRC
Crystal structure of phosphorylated AC3-AC5 domains of yeast acetyl-CoA carboxylase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 1601 |
| Chain | Residue |
| A | VAL1082 |
| A | PHE1083 |
| A | ARG1108 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 1601 |
| Chain | Residue |
| B | PHE1083 |
| B | ARG1108 |
| B | TYR1272 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15665377","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
