3GFS
Structure of YhdA, K109D/D137K variant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0005829 | cellular_component | cytosol |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042802 | molecular_function | identical protein binding |
| E | 0005829 | cellular_component | cytosol |
| E | 0010181 | molecular_function | FMN binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0042802 | molecular_function | identical protein binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0010181 | molecular_function | FMN binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0042802 | molecular_function | identical protein binding |
| G | 0005829 | cellular_component | cytosol |
| G | 0010181 | molecular_function | FMN binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0042802 | molecular_function | identical protein binding |
| H | 0005829 | cellular_component | cytosol |
| H | 0010181 | molecular_function | FMN binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0042802 | molecular_function | identical protein binding |
| I | 0005829 | cellular_component | cytosol |
| I | 0010181 | molecular_function | FMN binding |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0042802 | molecular_function | identical protein binding |
| J | 0005829 | cellular_component | cytosol |
| J | 0010181 | molecular_function | FMN binding |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0042802 | molecular_function | identical protein binding |
| K | 0005829 | cellular_component | cytosol |
| K | 0010181 | molecular_function | FMN binding |
| K | 0016491 | molecular_function | oxidoreductase activity |
| K | 0042802 | molecular_function | identical protein binding |
| L | 0005829 | cellular_component | cytosol |
| L | 0010181 | molecular_function | FMN binding |
| L | 0016491 | molecular_function | oxidoreductase activity |
| L | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN A 200 |
| Chain | Residue |
| A | THR9 |
| A | SER76 |
| A | VAL104 |
| A | ALA105 |
| A | GLY106 |
| A | GLY107 |
| A | GLY110 |
| A | HOH281 |
| C | ASP87 |
| A | ARG11 |
| A | GLY14 |
| A | ARG15 |
| A | THR16 |
| A | PRO72 |
| A | GLU73 |
| A | TYR74 |
| A | HIS75 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN B 200 |
| Chain | Residue |
| B | THR9 |
| B | ARG11 |
| B | GLY14 |
| B | ARG15 |
| B | THR16 |
| B | PRO72 |
| B | GLU73 |
| B | TYR74 |
| B | HIS75 |
| B | SER76 |
| B | VAL104 |
| B | ALA105 |
| B | GLY106 |
| B | GLY107 |
| B | GLY110 |
| D | ASP87 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN C 200 |
| Chain | Residue |
| A | ASP87 |
| C | THR9 |
| C | ARG11 |
| C | GLY14 |
| C | ARG15 |
| C | THR16 |
| C | PRO72 |
| C | GLU73 |
| C | TYR74 |
| C | HIS75 |
| C | SER76 |
| C | VAL104 |
| C | ALA105 |
| C | GLY106 |
| C | GLY107 |
| C | GLY110 |
| C | HOH576 |
| C | HOH616 |
| F | GLU50 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN D 200 |
| Chain | Residue |
| B | ASP87 |
| D | THR9 |
| D | ARG11 |
| D | GLY14 |
| D | ARG15 |
| D | THR16 |
| D | PRO72 |
| D | GLU73 |
| D | TYR74 |
| D | HIS75 |
| D | SER76 |
| D | VAL104 |
| D | ALA105 |
| D | GLY106 |
| D | GLY110 |
| D | HOH312 |
| E | HOH529 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN E 200 |
| Chain | Residue |
| E | THR9 |
| E | ARG11 |
| E | GLY14 |
| E | ARG15 |
| E | THR16 |
| E | PRO72 |
| E | GLU73 |
| E | TYR74 |
| E | HIS75 |
| E | SER76 |
| E | VAL104 |
| E | ALA105 |
| E | GLY106 |
| E | GLY107 |
| E | GLY110 |
| E | HOH581 |
| F | ASP87 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN F 200 |
| Chain | Residue |
| F | GLY106 |
| F | GLY107 |
| F | GLY110 |
| F | HOH482 |
| E | ASP87 |
| F | THR9 |
| F | ARG11 |
| F | GLY14 |
| F | ARG15 |
| F | THR16 |
| F | PRO72 |
| F | GLU73 |
| F | TYR74 |
| F | HIS75 |
| F | SER76 |
| F | VAL104 |
| F | ALA105 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE FMN G 200 |
| Chain | Residue |
| G | THR9 |
| G | ARG11 |
| G | GLY14 |
| G | ARG15 |
| G | THR16 |
| G | PRO72 |
| G | GLU73 |
| G | TYR74 |
| G | HIS75 |
| G | SER76 |
| G | VAL104 |
| G | ALA105 |
| G | GLY106 |
| G | GLY110 |
| G | HOH394 |
| H | ASP87 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN H 200 |
| Chain | Residue |
| G | ASP87 |
| H | THR9 |
| H | ARG11 |
| H | GLY14 |
| H | ARG15 |
| H | THR16 |
| H | PRO72 |
| H | GLU73 |
| H | TYR74 |
| H | HIS75 |
| H | SER76 |
| H | VAL104 |
| H | ALA105 |
| H | GLY106 |
| H | GLY107 |
| H | GLY110 |
| H | HOH692 |
| H | HOH940 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE FMN I 200 |
| Chain | Residue |
| I | THR9 |
| I | ARG11 |
| I | GLY14 |
| I | ARG15 |
| I | THR16 |
| I | PRO72 |
| I | GLU73 |
| I | TYR74 |
| I | HIS75 |
| I | SER76 |
| I | VAL104 |
| I | ALA105 |
| I | GLY106 |
| I | GLY107 |
| I | GLY110 |
| I | HOH422 |
| I | HOH463 |
| J | ASP87 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN J 200 |
| Chain | Residue |
| I | ASP87 |
| J | THR9 |
| J | ARG11 |
| J | GLY14 |
| J | ARG15 |
| J | THR16 |
| J | PRO72 |
| J | GLU73 |
| J | TYR74 |
| J | HIS75 |
| J | SER76 |
| J | VAL104 |
| J | ALA105 |
| J | GLY106 |
| J | GLY107 |
| J | GLY110 |
| J | HOH708 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FMN K 200 |
| Chain | Residue |
| K | THR9 |
| K | ARG11 |
| K | GLY14 |
| K | ARG15 |
| K | THR16 |
| K | PRO72 |
| K | GLU73 |
| K | TYR74 |
| K | HIS75 |
| K | SER76 |
| K | VAL104 |
| K | ALA105 |
| K | GLY106 |
| K | GLY107 |
| L | ASP87 |
| site_id | BC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE FMN L 200 |
| Chain | Residue |
| K | ASP87 |
| L | THR9 |
| L | ARG11 |
| L | GLY14 |
| L | ARG15 |
| L | THR16 |
| L | PRO72 |
| L | GLU73 |
| L | TYR74 |
| L | HIS75 |
| L | SER76 |
| L | VAL104 |
| L | ALA105 |
| L | GLY106 |
| L | GLY107 |
| L | GLY110 |
| L | HOH528 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 84 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JAN-2005","submissionDatabase":"PDB data bank","title":"Azobenzene reductase from Bacillus subtilis.","authoringGroup":["Midwest center for structural genomics (MCSG)"]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2008","submissionDatabase":"PDB data bank","title":"Crystal structure of the putative NADPH-dependent azobenzene FMN-reductase yhdA from Bacillus subtilis, Northeast structural genomics target SR135.","authoringGroup":["Northeast structural genomics consortium (NESG)"]}}]} |
| Chain | Residue | Details |






