6OJH
Crystal Structure of Haemophilus Influenzae Biotin Carboxylase Complexed with (R)-7-(3-aminopyrrolidin-1-yl)-6-(naphthalen-1-yl)pyrido[2,3-d]pyrimidin-2-amine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0004075 | molecular_function | biotin carboxylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006631 | biological_process | fatty acid metabolic process |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 2001295 | biological_process | malonyl-CoA biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | binding site for residue MV4 A 501 |
| Chain | Residue |
| A | ILE157 |
| A | GLU288 |
| A | ILE437 |
| A | HOH658 |
| A | LYS159 |
| A | MET169 |
| A | GLU201 |
| A | LYS202 |
| A | TYR203 |
| A | LEU204 |
| A | HIS236 |
| A | LEU278 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 502 |
| Chain | Residue |
| A | GLU276 |
| A | GLU288 |
| A | ASN290 |
| A | ACT503 |
| A | HOH695 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue ACT A 503 |
| Chain | Residue |
| A | GLU276 |
| A | GLU288 |
| A | ASN290 |
| A | ARG292 |
| A | CA502 |
| A | HOH610 |
| A | HOH658 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 444 |
| Details | Domain: {"description":"Biotin carboxylation"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 197 |
| Details | Domain: {"description":"ATP-grasp","evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P24182","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26020841","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MV8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26020841","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MV4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P24182","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26020841","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MV1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MV3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MV4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MV8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4RZQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
