Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE S1A A1567 |
| Chain | Residue |
| A | LYS73 |
| A | HOH2454 |
| B | ASN280 |
| A | ARG76 |
| A | SER77 |
| A | GLU392 |
| A | MET393 |
| A | ASN398 |
| A | TRP487 |
| A | PHE510 |
| A | HOH2453 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE S1A B1567 |
| Chain | Residue |
| B | LYS73 |
| B | ARG76 |
| B | SER77 |
| B | GLU392 |
| B | MET393 |
| B | VAL397 |
| B | ASN398 |
| B | TRP487 |
| B | PHE510 |
| B | HOH2508 |
| B | HOH2509 |
| B | HOH2510 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE S1A C1550 |
| Chain | Residue |
| C | LYS73 |
| C | ARG76 |
| C | SER77 |
| C | GLU392 |
| C | MET393 |
| C | VAL397 |
| C | ASN398 |
| C | TRP487 |
| C | PHE510 |
| C | HOH2480 |
| C | HOH2481 |
Functional Information from PROSITE/UniProt
| site_id | PS00866 |
| Number of Residues | 15 |
| Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. FPVMIKASeggGGkG |
| Chain | Residue | Details |
| A | PHE247-GLY261 | |
| site_id | PS00867 |
| Number of Residues | 8 |
| Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FLELNPRL |
| Chain | Residue | Details |
| A | PHE377-LEU384 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG383 | |
| B | ARG383 | |
| C | ARG383 | |
| Chain | Residue | Details |
| A | GLY256 | |
| B | GLY256 | |
| C | GLY256 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU365 | |
| A | GLU379 | |
| A | ASN381 | |
| B | GLU365 | |
| B | GLU379 | |
| B | ASN381 | |
| C | GLU365 | |
| C | GLU379 | |
| C | ASN381 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1gsa |
| Chain | Residue | Details |
| A | GLN302 | |
| A | ARG317 | |
| A | LYS252 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1gsa |
| Chain | Residue | Details |
| B | GLN302 | |
| B | ARG317 | |
| B | LYS252 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1gsa |
| Chain | Residue | Details |
| C | GLN302 | |
| C | ARG317 | |
| C | LYS252 | |
