2W6Z
Crystal structure of Biotin carboxylase from E. coli in complex with the 3-(3-Methyl-but-2-enyl)-3H-purin-6-ylamine fragment
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 | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006629 | biological_process | lipid metabolic process |
A | 0006631 | biological_process | fatty acid metabolic process |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
A | 0016874 | molecular_function | ligase activity |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0045717 | biological_process | negative regulation of fatty acid biosynthetic process |
A | 0046872 | molecular_function | metal ion binding |
A | 2001295 | biological_process | malonyl-CoA biosynthetic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
B | 0004075 | molecular_function | biotin carboxylase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006629 | biological_process | lipid metabolic process |
B | 0006631 | biological_process | fatty acid metabolic process |
B | 0006633 | biological_process | fatty acid biosynthetic process |
B | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
B | 0016874 | molecular_function | ligase activity |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0045717 | biological_process | negative regulation of fatty acid biosynthetic process |
B | 0046872 | molecular_function | metal ion binding |
B | 2001295 | biological_process | malonyl-CoA biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE L21 A 1447 |
Chain | Residue |
A | ILE157 |
A | LYS159 |
A | GLU201 |
A | LYS202 |
A | TYR203 |
A | LEU204 |
A | LEU278 |
A | ILE437 |
A | HIS438 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 1448 |
Chain | Residue |
A | ARG292 |
A | GLN294 |
A | VAL295 |
A | HOH2200 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 1446 |
Chain | Residue |
B | ARG292 |
B | GLN294 |
B | VAL295 |
B | HOH2124 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 888 |
Details | Domain: {"description":"Biotin carboxylation"} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 394 |
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 | 2 |
Details | Active site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8D","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"10821865","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19213731","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DV2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3G8C","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00409","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |