4MV8
Crystal Structure of Biotin Carboxylase from Haemophilus influenzae in Complex with AMPPCP and Phosphate
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 | 6 | 
| Details | BINDING SITE FOR RESIDUE PO4 A 501 | 
| Chain | Residue | 
| A | LYS238 | 
| A | ARG292 | 
| A | GLN294 | 
| A | VAL295 | 
| A | GLU296 | 
| A | ARG338 | 
| site_id | AC2 | 
| Number of Residues | 11 | 
| Details | BINDING SITE FOR RESIDUE ACP A 502 | 
| Chain | Residue | 
| A | GLU201 | 
| A | LYS202 | 
| A | LEU204 | 
| A | HIS236 | 
| A | GLU276 | 
| A | LEU278 | 
| A | ASN290 | 
| A | ILE437 | 
| A | LYS116 | 
| A | LYS159 | 
| A | MET169 | 
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 1 | 
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P24182","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| 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_FI3 | 
| 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_FI4 | 
| 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_FI5 | 
| Number of Residues | 6 | 
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P24182","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI6 | 
| Number of Residues | 3 | 
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 











