3WGG
Crystal structure of RSP in complex with alpha-NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003700 | molecular_function | DNA-binding transcription factor activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006351 | biological_process | DNA-templated transcription |
| A | 0006355 | biological_process | regulation of DNA-templated transcription |
| A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051775 | biological_process | response to redox state |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003700 | molecular_function | DNA-binding transcription factor activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006351 | biological_process | DNA-templated transcription |
| B | 0006355 | biological_process | regulation of DNA-templated transcription |
| B | 0045892 | biological_process | negative regulation of DNA-templated transcription |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051775 | biological_process | response to redox state |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE 8NA A 301 |
| Chain | Residue |
| A | ILE90 |
| A | PRO155 |
| A | ASN158 |
| A | THR162 |
| A | PHE177 |
| A | PRO179 |
| A | SO4303 |
| A | HOH427 |
| A | HOH498 |
| A | HOH530 |
| A | HOH542 |
| A | GLY93 |
| A | HOH547 |
| A | HOH559 |
| B | ASN101 |
| B | TYR102 |
| B | THR103 |
| B | SER104 |
| A | ASN94 |
| A | LEU95 |
| A | ASP117 |
| A | ILE118 |
| A | ASN119 |
| A | CYS153 |
| A | ILE154 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | ARG17 |
| A | ARG20 |
| A | TYR21 |
| A | HOH410 |
| B | ASN192 |
| B | HIS194 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | PRO179 |
| A | HIS194 |
| A | LEU195 |
| A | SER196 |
| A | 8NA301 |
| A | HOH408 |
| B | TYR102 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | SER34 |
| A | SER35 |
| A | GLN61 |
| A | GLY63 |
| A | TYR64 |
| A | GLY65 |
| A | HOH520 |
| A | HOH521 |
| site_id | AC5 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE 8NA B 301 |
| Chain | Residue |
| A | GLN61 |
| A | ASN101 |
| A | TYR102 |
| A | THR103 |
| A | SER104 |
| A | HOH418 |
| B | ILE90 |
| B | GLY93 |
| B | ASN94 |
| B | LEU95 |
| B | ASP117 |
| B | ILE118 |
| B | ASN119 |
| B | LEU122 |
| B | CYS153 |
| B | ILE154 |
| B | PRO155 |
| B | PHE177 |
| B | PRO179 |
| B | SO4302 |
| B | HOH451 |
| B | HOH453 |
| B | HOH454 |
| B | HOH455 |
| B | HOH456 |
| B | HOH464 |
| B | HOH538 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 302 |
| Chain | Residue |
| A | TYR102 |
| B | HIS194 |
| B | LEU195 |
| B | SER196 |
| B | 8NA301 |
| B | HOH449 |
| B | HOH483 |
| B | HOH617 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 303 |
| Chain | Residue |
| B | SER34 |
| B | SER35 |
| B | ARG36 |
| B | ARG50 |
| B | GLY65 |
| B | PRO185 |
| B | HOH411 |
| B | HOH559 |
| B | HOH594 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 304 |
| Chain | Residue |
| A | HIS194 |
| B | ARG20 |
| B | HOH413 |
| B | HOH466 |
