3M0E
Crystal structure of the ATP-bound state of Walker B mutant of NtrC1 ATPase domain
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 | 19 |
| Details | BINDING SITE FOR RESIDUE ATP A 400 |
| Chain | Residue |
| A | HOH16 |
| A | LYS173 |
| A | GLU174 |
| A | VAL175 |
| A | ASN280 |
| A | LEU320 |
| A | VAL356 |
| A | ARG357 |
| A | MG401 |
| B | ASP295 |
| B | ARG299 |
| A | HOH49 |
| A | HOH98 |
| A | TYR139 |
| A | VAL140 |
| A | SER169 |
| A | GLY170 |
| A | VAL171 |
| A | GLY172 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | HOH16 |
| A | GLU174 |
| A | ASP238 |
| A | ATP400 |
| A | HOH416 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP B 400 |
| Chain | Residue |
| B | HOH14 |
| B | HOH114 |
| B | TYR139 |
| B | VAL140 |
| B | SER169 |
| B | GLY170 |
| B | VAL171 |
| B | GLY172 |
| B | LYS173 |
| B | GLU174 |
| B | VAL175 |
| B | ASN280 |
| B | VAL356 |
| B | ARG357 |
| B | MG401 |
| B | HOH427 |
| C | ASP295 |
| C | ARG299 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 401 |
| Chain | Residue |
| B | HOH14 |
| B | GLU174 |
| B | ATP400 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP C 400 |
| Chain | Residue |
| C | HOH19 |
| C | HOH43 |
| C | TYR139 |
| C | VAL140 |
| C | SER169 |
| C | GLY170 |
| C | VAL171 |
| C | GLY172 |
| C | LYS173 |
| C | GLU174 |
| C | VAL175 |
| C | ASN280 |
| C | VAL356 |
| C | ARG357 |
| C | MG401 |
| D | ASP295 |
| D | ARG299 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 401 |
| Chain | Residue |
| C | HOH19 |
| C | GLU174 |
| C | ASP238 |
| C | ATP400 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE ATP D 400 |
| Chain | Residue |
| D | TYR139 |
| D | VAL140 |
| D | SER169 |
| D | GLY170 |
| D | VAL171 |
| D | GLY172 |
| D | LYS173 |
| D | GLU174 |
| D | VAL175 |
| D | ASN280 |
| D | LEU320 |
| D | VAL356 |
| D | ARG357 |
| D | MG401 |
| D | HOH410 |
| E | HOH8 |
| E | ASP295 |
| E | ARG299 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 401 |
| Chain | Residue |
| D | GLU174 |
| D | ASP238 |
| D | ATP400 |
| E | HOH8 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP E 400 |
| Chain | Residue |
| E | ASN280 |
| E | LEU320 |
| E | VAL356 |
| E | ARG357 |
| E | HOH395 |
| E | MG401 |
| F | ASP295 |
| F | ARG299 |
| E | HOH6 |
| E | HOH68 |
| E | TYR139 |
| E | VAL140 |
| E | SER169 |
| E | GLY170 |
| E | VAL171 |
| E | GLY172 |
| E | LYS173 |
| E | GLU174 |
| E | VAL175 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 401 |
| Chain | Residue |
| E | HOH6 |
| E | GLU174 |
| E | ATP400 |
| E | HOH405 |
| F | ARG299 |
| site_id | BC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ATP F 400 |
| Chain | Residue |
| F | HOH18 |
| F | HOH40 |
| F | TYR139 |
| F | VAL140 |
| F | SER169 |
| F | GLY170 |
| F | VAL171 |
| F | GLY172 |
| F | LYS173 |
| F | GLU174 |
| F | VAL175 |
| F | ASN280 |
| F | VAL356 |
| F | ARG357 |
| F | MG401 |
| G | ASP295 |
| G | ARG299 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 401 |
| Chain | Residue |
| F | HOH18 |
| F | GLU174 |
| F | ASP238 |
| F | ATP400 |
| F | HOH419 |
| site_id | BC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ATP G 400 |
| Chain | Residue |
| A | ASP295 |
| A | ARG299 |
| G | HOH7 |
| G | HOH35 |
| G | TYR139 |
| G | VAL140 |
| G | SER169 |
| G | GLY170 |
| G | VAL171 |
| G | GLY172 |
| G | LYS173 |
| G | GLU174 |
| G | VAL175 |
| G | ASN280 |
| G | LEU320 |
| G | VAL356 |
| G | ARG357 |
| G | HOH388 |
| G | MG401 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 401 |
| Chain | Residue |
| G | HOH7 |
| G | GLU174 |
| G | ASP238 |
| G | ATP400 |
| G | HOH422 |
Functional Information from PROSITE/UniProt
| site_id | PS00675 |
| Number of Residues | 14 |
| Details | SIGMA54_INTERACT_1 Sigma-54 interaction domain ATP-binding region A signature. VLItGESGVGKevV |
| Chain | Residue | Details |
| A | VAL163-VAL176 |
