4QHT
Crystal structure of AAA+/ sigma 54 activator domain of the flagellar regulatory protein FlrC from Vibrio cholerae in ATP analog bound 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 | 20 |
| Details | BINDING SITE FOR RESIDUE ANP A 401 |
| Chain | Residue |
| A | MET131 |
| A | VAL167 |
| A | ASN272 |
| A | LEU312 |
| A | ARG319 |
| A | VAL348 |
| A | ARG349 |
| A | MG402 |
| A | HOH501 |
| A | HOH522 |
| A | HOH531 |
| A | VAL132 |
| A | HOH551 |
| A | PRO160 |
| A | SER161 |
| A | GLY162 |
| A | SER163 |
| A | GLY164 |
| A | LYS165 |
| A | GLU166 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | ASN187 |
| A | ASP230 |
| A | ANP401 |
| A | HOH531 |
| A | HOH547 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 403 |
| Chain | Residue |
| A | ARG285 |
| A | GLU286 |
| A | ASP287 |
| A | HOH545 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 404 |
| Chain | Residue |
| A | VAL265 |
| A | HOH507 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ANP B 401 |
| Chain | Residue |
| B | MET131 |
| B | VAL132 |
| B | SER161 |
| B | GLY162 |
| B | SER163 |
| B | GLY164 |
| B | LYS165 |
| B | GLU166 |
| B | VAL167 |
| B | GLU231 |
| B | ASN272 |
| B | LEU312 |
| B | ARG319 |
| B | VAL348 |
| B | ARG349 |
| B | MG402 |
| B | HOH501 |
| B | HOH511 |
| B | HOH543 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 402 |
| Chain | Residue |
| B | ASP230 |
| B | GLU231 |
| B | ANP401 |
| B | HOH501 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 403 |
| Chain | Residue |
| B | LEU247 |
| B | ARG250 |
| B | VAL265 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE ANP C 401 |
| Chain | Residue |
| C | MET131 |
| C | VAL132 |
| C | SER161 |
| C | GLY162 |
| C | SER163 |
| C | GLY164 |
| C | LYS165 |
| C | GLU166 |
| C | VAL167 |
| C | GLU231 |
| C | ASN272 |
| C | LEU312 |
| C | ARG319 |
| C | VAL348 |
| C | ARG349 |
| C | MG402 |
| C | HOH528 |
| C | HOH531 |
| C | HOH532 |
| C | HOH533 |
| C | HOH551 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 402 |
| Chain | Residue |
| C | ASN187 |
| C | ASP230 |
| C | GLU231 |
| C | ANP401 |
| C | HOH551 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 403 |
| Chain | Residue |
| C | ARG285 |
| C | GLU286 |
| C | ASP287 |
| C | HOH535 |
| C | HOH569 |
| site_id | BC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ANP D 401 |
| Chain | Residue |
| D | LEU312 |
| D | HIS315 |
| D | ARG319 |
| D | VAL348 |
| D | ARG349 |
| D | MG402 |
| D | HOH533 |
| D | HOH538 |
| D | HOH548 |
| D | MET131 |
| D | VAL132 |
| D | PRO160 |
| D | SER161 |
| D | GLY162 |
| D | SER163 |
| D | GLY164 |
| D | LYS165 |
| D | GLU166 |
| D | VAL167 |
| D | ASN272 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 402 |
| Chain | Residue |
| D | ASP230 |
| D | ANP401 |
| D | HOH538 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 403 |
| Chain | Residue |
| D | ARG285 |
| D | GLU286 |
| D | ASP287 |
| D | HOH536 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 404 |
| Chain | Residue |
| D | ASN154 |
| D | LEU247 |
| D | ARG250 |
| D | VAL265 |
| D | HOH504 |
| site_id | BC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ANP E 401 |
| Chain | Residue |
| E | MET131 |
| E | VAL132 |
| E | PRO160 |
| E | SER161 |
| E | GLY162 |
| E | SER163 |
| E | GLY164 |
| E | LYS165 |
| E | GLU166 |
| E | VAL167 |
| E | ASN272 |
| E | LEU312 |
| E | HIS315 |
| E | ARG319 |
| E | VAL348 |
| E | ARG349 |
| E | MG402 |
| E | HOH510 |
| E | HOH535 |
| E | HOH564 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 402 |
| Chain | Residue |
| E | ASN187 |
| E | ASP230 |
| E | ANP401 |
| E | HOH510 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO E 403 |
| Chain | Residue |
| E | ARG285 |
| E | GLU286 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO E 404 |
| Chain | Residue |
| E | LEU247 |
| E | ARG250 |
| E | VAL265 |
| site_id | CC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ANP F 401 |
| Chain | Residue |
| F | MET131 |
| F | VAL132 |
| F | SER161 |
| F | GLY162 |
| F | SER163 |
| F | GLY164 |
| F | LYS165 |
| F | GLU166 |
| F | VAL167 |
| F | ASN272 |
| F | LEU312 |
| F | ARG319 |
| F | VAL348 |
| F | ARG349 |
| F | MG402 |
| F | HOH501 |
| F | HOH522 |
| F | HOH525 |
| F | HOH530 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 402 |
| Chain | Residue |
| F | ASP230 |
| F | ANP401 |
| F | HOH522 |
| F | HOH530 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO F 403 |
| Chain | Residue |
| E | HOH564 |
| F | ARG285 |
| F | GLU286 |
| F | ASP287 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO F 404 |
| Chain | Residue |
| F | LEU247 |
| F | ARG250 |
| F | VAL265 |
| site_id | CC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ANP G 401 |
| Chain | Residue |
| G | HIS130 |
| G | MET131 |
| G | VAL132 |
| G | SER161 |
| G | GLY162 |
| G | SER163 |
| G | GLY164 |
| G | LYS165 |
| G | GLU166 |
| G | VAL167 |
| G | ASN272 |
| G | LEU312 |
| G | ARG319 |
| G | VAL348 |
| G | ARG349 |
| G | MG402 |
| G | HOH534 |
| G | HOH535 |
| G | HOH547 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG G 402 |
| Chain | Residue |
| G | ASP230 |
| G | ANP401 |
| G | HOH534 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO G 403 |
| Chain | Residue |
| G | ARG285 |
| G | GLU286 |
| G | HOH539 |
| G | HOH540 |
| site_id | CC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO G 404 |
| Chain | Residue |
| G | ARG250 |
| G | VAL265 |
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 |
