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 | 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 | 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 | 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 | 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 | 76 |
Details | DNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00307 |
Chain | Residue | Details |
A | LYS42-GLN61 | |
B | LYS42-GLN61 | |
C | LYS42-GLN61 | |
D | LYS42-GLN61 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250 |
Chain | Residue | Details |
A | LYS312 | |
B | LYS312 | |
C | LYS312 | |
D | LYS312 |