6OI8
Crystal Structure of Haemophilus Influenzae Biotin Carboxylase Complexed with 7-((1R,5S,6s)-6-amino-3-azabicyclo[3.1.0]hexan-3-yl)-6-(2-chloro-6-(pyridin-3-yl)phenyl)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 | 5 |
Details | binding site for residue EDO A 501 |
Chain | Residue |
A | PRO349 |
A | PRO378 |
A | PRO379 |
A | TYR381 |
A | ASP382 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue MQV A 502 |
Chain | Residue |
A | LYS202 |
A | TYR203 |
A | LEU204 |
A | GLN233 |
A | HIS236 |
A | GLU276 |
A | LEU278 |
A | GLU288 |
A | ILE437 |
A | ILE157 |
A | LYS159 |
A | MET169 |
A | GLU201 |
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 |