4MGR
The crystal structure of Bacillus subtilis GabR, an autorepressor and PLP- and GABA-dependent transcriptional activator of gabT
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009058 | biological_process | biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009058 | biological_process | biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0003677 | molecular_function | DNA binding |
| C | 0003700 | molecular_function | DNA-binding transcription factor activity |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009058 | biological_process | biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0003677 | molecular_function | DNA binding |
| D | 0003700 | molecular_function | DNA-binding transcription factor activity |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009058 | biological_process | biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | ASN303 |
| A | HOH610 |
| A | HOH611 |
| A | HOH619 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD A 502 |
| Chain | Residue |
| A | TYR205 |
| A | ASP279 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 503 |
| Chain | Residue |
| A | GLY337 |
| A | PRO148 |
| A | TYR333 |
| A | LYS334 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | ASN303 |
| B | HOH685 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE IMD B 502 |
| Chain | Residue |
| B | TYR205 |
| B | ASP279 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACT B 503 |
| Chain | Residue |
| B | PRO148 |
| B | ILE177 |
| B | GLY178 |
| B | LEU340 |
| B | GLN341 |
| B | THR342 |
| B | HOH663 |
| B | HOH689 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 504 |
| Chain | Residue |
| B | TYR333 |
| B | LYS334 |
| B | GLY337 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 505 |
| Chain | Residue |
| B | HIS114 |
| B | TYR205 |
| B | ARG207 |
| B | ARG430 |
| B | PHE431 |
| B | HOH668 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 506 |
| Chain | Residue |
| B | GLU389 |
| C | GLY470 |
| C | LYS472 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| B | ASP97 |
| C | ASN303 |
| C | HOH722 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD C 502 |
| Chain | Residue |
| C | TYR205 |
| C | PHE250 |
| C | ASP279 |
| C | HOH702 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT C 503 |
| Chain | Residue |
| C | PRO148 |
| C | TYR333 |
| C | ARG336 |
| C | GLY337 |
| C | ASP339 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT C 504 |
| Chain | Residue |
| B | GLU385 |
| B | GLN462 |
| C | GLU385 |
| C | HOH681 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 501 |
| Chain | Residue |
| D | ASN303 |
| D | HOH657 |
| D | HOH701 |
| D | HOH714 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IMD D 502 |
| Chain | Residue |
| D | TYR205 |
| D | PHE250 |
| D | ASP279 |
| D | TYR281 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT D 503 |
| Chain | Residue |
| D | PRO148 |
| D | TYR333 |
| D | LYS334 |
| D | GLY337 |
| D | TYR338 |
| D | ASP339 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 504 |
| Chain | Residue |
| D | ASP144 |
| D | GLU153 |
| D | HOH685 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 272 |
| Details | Domain: {"description":"HTH gntR-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00307","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 76 |
| Details | DNA binding: {"description":"H-T-H motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00307","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
