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 | MOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER1148 | |
B | SER1148 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SEP1157 | |
B | SEP1157 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | SER1162 | |
B | SER1162 |