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 |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0008134 | molecular_function | transcription factor binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006355 | biological_process | regulation of DNA-templated transcription |
| C | 0008134 | molecular_function | transcription factor binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0008134 | molecular_function | transcription factor binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006355 | biological_process | regulation of DNA-templated transcription |
| E | 0008134 | molecular_function | transcription factor binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006355 | biological_process | regulation of DNA-templated transcription |
| F | 0008134 | molecular_function | transcription factor binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006355 | biological_process | regulation of DNA-templated transcription |
| G | 0008134 | molecular_function | transcription factor binding |
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 |
