8DLE
Crosslinked Crystal Structure of the 8-amino-7-oxonanoate synthase, BioF, and Benzene Sulfonyl Fluoride-crypto Acyl Carrier Protein, BSF-ACP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008710 | molecular_function | 8-amino-7-oxononanoate synthase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0000035 | molecular_function | acyl binding |
| B | 0000036 | molecular_function | acyl carrier activity |
| B | 0005515 | molecular_function | protein 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 | 0008289 | molecular_function | lipid binding |
| B | 0008610 | biological_process | lipid biosynthetic process |
| B | 0009245 | biological_process | lipid A biosynthetic process |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0016020 | cellular_component | membrane |
| B | 0031177 | molecular_function | phosphopantetheine binding |
Functional Information from PROSITE/UniProt
| site_id | PS00012 |
| Number of Residues | 16 |
| Details | PHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGADSLDTVELVMAL |
| Chain | Residue | Details |
| B | ASP31-LEU46 |
| site_id | PS00599 |
| Number of Residues | 10 |
| Details | AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFGKGFGVSG |
| Chain | Residue | Details |
| A | THR233-GLY242 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10642176","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10642176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16557306","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10642176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16557306","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 75 |
| Details | Domain: {"description":"Carrier","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"4882207","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 430 |
| Chain | Residue | Details |
| A | ASN47 | electrostatic stabiliser |
| A | HIS133 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | GLU175 | electrostatic stabiliser |
| A | SER179 | modifies pKa |
| A | ASP204 | electrostatic stabiliser |
| A | HIS207 | electrostatic stabiliser, proton shuttle (general acid/base) |
| A | LYS236 | covalent catalysis, proton shuttle (general acid/base) |
