1R30
The Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004076 | molecular_function | biotin synthase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0009102 | biological_process | biotin biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042364 | biological_process | water-soluble vitamin biosynthetic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0044272 | biological_process | sulfur compound biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004076 | molecular_function | biotin synthase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0009102 | biological_process | biotin biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042364 | biological_process | water-soluble vitamin biosynthetic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0044272 | biological_process | sulfur compound biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAM A 501 |
| Chain | Residue |
| A | TYR59 |
| A | LEU224 |
| A | VAL225 |
| A | LEU291 |
| A | SF4401 |
| A | DTB502 |
| A | PRO61 |
| A | ALA100 |
| A | TRP102 |
| A | GLY132 |
| A | ASN153 |
| A | ASP155 |
| A | ARG173 |
| A | ILE192 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAM B 501 |
| Chain | Residue |
| B | TYR59 |
| B | ALA100 |
| B | TRP102 |
| B | GLY132 |
| B | ASN153 |
| B | ASP155 |
| B | ARG173 |
| B | ILE192 |
| B | MET223 |
| B | LEU224 |
| B | VAL225 |
| B | LEU291 |
| B | SF4401 |
| B | DTB502 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SF4 A 401 |
| Chain | Residue |
| A | CYS53 |
| A | GLU55 |
| A | CYS57 |
| A | CYS60 |
| A | SAM501 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FES A 402 |
| Chain | Residue |
| A | CYS97 |
| A | CYS128 |
| A | CYS188 |
| A | ARG260 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SF4 B 401 |
| Chain | Residue |
| B | CYS53 |
| B | CYS57 |
| B | CYS60 |
| B | SAM501 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FES B 402 |
| Chain | Residue |
| B | ARG95 |
| B | CYS97 |
| B | CYS128 |
| B | CYS188 |
| B | ARG260 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DTB A 502 |
| Chain | Residue |
| A | LEU45 |
| A | ASN151 |
| A | ASN153 |
| A | ASN222 |
| A | ALA263 |
| A | PHE285 |
| A | LEU291 |
| A | THR292 |
| A | THR293 |
| A | SAM501 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DTB B 502 |
| Chain | Residue |
| B | ASN151 |
| B | ASN153 |
| B | ASN222 |
| B | ALA263 |
| B | PHE285 |
| B | LEU290 |
| B | LEU291 |
| B | THR292 |
| B | THR293 |
| B | SAM501 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE TRS A 503 |
| Chain | Residue |
| A | LYS121 |
| A | ALA143 |
| A | GLU266 |
| A | GLU297 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | CYS53 | |
| B | CYS60 | |
| B | CYS97 | |
| B | CYS128 | |
| B | CYS188 | |
| B | ARG260 | |
| A | CYS57 | |
| A | CYS60 | |
| A | CYS97 | |
| A | CYS128 | |
| A | CYS188 | |
| A | ARG260 | |
| B | CYS53 | |
| B | CYS57 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11862544, 11834738, 14967042, 14704425 |
| Chain | Residue | Details |
| A | CYS60 | |
| A | CYS53 | |
| A | CYS57 | |
| A | ARG260 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 11862544, 11834738, 14967042, 14704425 |
| Chain | Residue | Details |
| B | CYS60 | |
| B | CYS53 | |
| B | CYS57 | |
| B | ARG260 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 767 |
| Chain | Residue | Details |
| A | CYS53 | electrostatic stabiliser, metal ligand |
| A | CYS57 | electrostatic stabiliser, metal ligand |
| A | CYS60 | electrostatic stabiliser, metal ligand |
| A | CYS97 | metal ligand |
| A | CYS128 | metal ligand |
| A | CYS188 | metal ligand |
| A | ARG260 | alter redox potential, electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 767 |
| Chain | Residue | Details |
| B | CYS53 | electrostatic stabiliser, metal ligand |
| B | CYS57 | electrostatic stabiliser, metal ligand |
| B | CYS60 | electrostatic stabiliser, metal ligand |
| B | CYS97 | metal ligand |
| B | CYS128 | metal ligand |
| B | CYS188 | metal ligand |
| B | ARG260 | alter redox potential, electrostatic stabiliser |
