4ASI
Crystal structure of human ACACA C-terminal domain
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0016874 | molecular_function | ligase activity |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0016874 | molecular_function | ligase activity |
| C | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| C | 0016874 | molecular_function | ligase activity |
| D | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| D | 0016874 | molecular_function | ligase activity |
| E | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| E | 0016874 | molecular_function | ligase activity |
| F | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| F | 0016874 | molecular_function | ligase activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1896 |
| Details | Domain: {"description":"CoA carboxyltransferase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU01137","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
