2YL2
Crystal structure of human acetyl-CoA carboxylase 1, biotin carboxylase (BC) domain
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 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG478 | |
| B | ARG478 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 |
| Chain | Residue | Details |
| A | GLY352 | |
| B | GLY352 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969 |
| Chain | Residue | Details |
| A | GLU461 | |
| A | GLU474 | |
| A | ASN476 | |
| B | GLU461 | |
| B | GLU474 | |
| B | ASN476 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11497 |
| Chain | Residue | Details |
| A | SER115 | |
| B | SER115 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:29899443, ECO:0000269|Ref.9, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER117 | |
| B | SER117 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336 |
| Chain | Residue | Details |
| A | SER525 | |
| B | SER525 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | THR647 | |
| B | THR647 |
