4N0B
Crystal structure of Bacillus subtilis GabR, an autorepressor and 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 | 5 |
Details | BINDING SITE FOR RESIDUE ACE A 501 |
Chain | Residue |
A | TYR205 |
A | ARG206 |
A | ARG207 |
A | ARG430 |
A | PHE431 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 502 |
Chain | Residue |
A | ASN303 |
A | HOH616 |
A | HOH617 |
D | PRO96 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACE B 501 |
Chain | Residue |
B | HIS114 |
B | TYR205 |
B | ARG206 |
B | ARG207 |
B | PHE431 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 502 |
Chain | Residue |
B | ARG273 |
B | ASN303 |
B | HOH620 |
B | HOH621 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 501 |
Chain | Residue |
C | ASN303 |
C | HOH608 |
C | HOH609 |
C | HOH610 |
site_id | AC6 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CA D 501 |
Chain | Residue |
D | GLU270 |
D | GLU376 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE ZN D 502 |
Chain | Residue |
D | ASN303 |
D | HOH607 |
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 | LLP312 | |
B | LLP312 | |
C | LLP312 | |
D | LLP312 |