Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 401 |
Chain | Residue |
A | ARG23 |
A | ARG101 |
A | LEU256 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 402 |
Chain | Residue |
A | LEU147 |
A | ARG148 |
A | ARG149 |
A | HOH1168 |
A | HOH1218 |
A | HOH1430 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 A 403 |
Chain | Residue |
A | ARG130 |
A | ALA151 |
A | HIS152 |
A | HOH1093 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PLP A 400 |
Chain | Residue |
A | SER107 |
A | GLY108 |
A | PHE109 |
A | HIS133 |
A | GLU175 |
A | SER179 |
A | ASP204 |
A | ALA206 |
A | HIS207 |
A | THR233 |
A | LYS236 |
A | SER265 |
A | THR266 |
A | HOH1030 |
A | HOH1117 |
A | HOH1290 |
A | HOH1340 |
Functional Information from PROSITE/UniProt
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
Chain | Residue | Details |
A | ARG21 | |
A | HIS133 | |
A | THR233 | |
A | THR352 | |
Chain | Residue | Details |
A | GLY108 | |
A | SER179 | |
A | HIS207 | |
Chain | Residue | Details |
A | LYS236 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
A | ASP204 | |
A | GLU175 | |
A | LYS236 | |
A | HIS133 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
A | HIS207 | |
A | PHE238 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1bs0 |
Chain | Residue | Details |
A | HIS207 | |
A | LYS236 | |
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) |