6LUF
Trans-acting mutant Y290A of the central AAA+ domain of the flagellar regulatory protein FlrC
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0008134 | molecular_function | transcription factor binding |
A | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006355 | biological_process | regulation of DNA-templated transcription |
B | 0008134 | molecular_function | transcription factor binding |
B | 0016887 | molecular_function | ATP hydrolysis activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006355 | biological_process | regulation of DNA-templated transcription |
C | 0008134 | molecular_function | transcription factor binding |
C | 0016887 | molecular_function | ATP hydrolysis activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0008134 | molecular_function | transcription factor binding |
D | 0016887 | molecular_function | ATP hydrolysis activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006355 | biological_process | regulation of DNA-templated transcription |
E | 0008134 | molecular_function | transcription factor binding |
E | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006355 | biological_process | regulation of DNA-templated transcription |
F | 0008134 | molecular_function | transcription factor binding |
F | 0016887 | molecular_function | ATP hydrolysis activity |
G | 0005524 | molecular_function | ATP binding |
G | 0006355 | biological_process | regulation of DNA-templated transcription |
G | 0008134 | molecular_function | transcription factor binding |
G | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | binding site for residue ADP A 401 |
Chain | Residue |
A | VAL132 |
A | ARG319 |
A | VAL348 |
A | GLY162 |
A | SER163 |
A | GLY164 |
A | LYS165 |
A | GLU166 |
A | VAL167 |
A | TRP299 |
A | LEU312 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue ADP B 401 |
Chain | Residue |
B | HIS130 |
B | VAL132 |
B | SER161 |
B | GLY162 |
B | SER163 |
B | GLY164 |
B | LYS165 |
B | GLU166 |
B | VAL167 |
B | ARG319 |
B | VAL348 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue ADP C 401 |
Chain | Residue |
C | VAL132 |
C | SER161 |
C | GLY162 |
C | SER163 |
C | GLY164 |
C | LYS165 |
C | GLU166 |
C | VAL167 |
C | TRP299 |
C | LEU312 |
C | ARG319 |
C | VAL348 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue ADP D 401 |
Chain | Residue |
D | VAL132 |
D | GLY162 |
D | SER163 |
D | GLY164 |
D | LYS165 |
D | GLU166 |
D | ASP230 |
D | ARG305 |
D | LEU312 |
D | ARG319 |
D | VAL348 |
site_id | AC5 |
Number of Residues | 13 |
Details | binding site for residue ADP E 401 |
Chain | Residue |
E | MET131 |
E | VAL133 |
E | SER161 |
E | GLY162 |
E | SER163 |
E | GLY164 |
E | LYS165 |
E | GLU166 |
E | VAL167 |
E | TRP299 |
E | LEU312 |
E | ARG319 |
E | VAL348 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue ADP F 401 |
Chain | Residue |
F | MET131 |
F | VAL132 |
F | SER161 |
F | GLY162 |
F | SER163 |
F | GLY164 |
F | LYS165 |
F | ASP230 |
F | TRP299 |
F | LEU312 |
F | ARG319 |
F | VAL348 |
site_id | AC7 |
Number of Residues | 8 |
Details | binding site for residue ADP G 401 |
Chain | Residue |
G | GLY162 |
G | SER163 |
G | GLY164 |
G | LYS165 |
G | GLU166 |
G | LEU312 |
G | ARG319 |
G | VAL348 |
Functional Information from PROSITE/UniProt
site_id | PS00676 |
Number of Residues | 16 |
Details | SIGMA54_INTERACT_2 Sigma-54 interaction domain ATP-binding region B signature. GkFeqAQGGTILLDEI |
Chain | Residue | Details |
A | GLY217-ILE232 |
site_id | PS00688 |
Number of Residues | 10 |
Details | SIGMA54_INTERACT_3 Sigma-54 interaction domain C-terminal part signature. WPGNVRELdN |
Chain | Residue | Details |
A | TRP344-ASN353 |