4QHS
Crystal structure of AAA+sigma 54 activator domain of the flagellar regulatory protein FlrC of Vibrio cholerae in nucleotide free state
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 | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 401 |
Chain | Residue |
A | ARG285 |
A | GLU286 |
A | ASP287 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 401 |
Chain | Residue |
C | ARG285 |
C | GLU286 |
C | ASP287 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO B 401 |
Chain | Residue |
B | HOH605 |
B | ARG285 |
B | GLU286 |
B | ASP287 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO F 401 |
Chain | Residue |
F | ARG285 |
F | GLU286 |
F | ASP287 |
F | HOH522 |
F | HOH582 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO G 401 |
Chain | Residue |
G | ARG285 |
G | GLU286 |
G | ASP287 |
G | HOH622 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO E 401 |
Chain | Residue |
E | ARG285 |
E | GLU286 |
E | ASP287 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO D 401 |
Chain | Residue |
D | ARG285 |
D | GLU286 |
D | ASP287 |
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 |