3WGH
Crystal structure of RSP in complex with beta-NADH
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 | 22 |
| Details | BINDING SITE FOR RESIDUE NAI A 301 |
| Chain | Residue |
| A | ILE90 |
| A | PRO155 |
| A | THR162 |
| A | PHE177 |
| A | LEU178 |
| A | VAL193 |
| A | LEU195 |
| A | HOH509 |
| A | HOH518 |
| A | HOH550 |
| A | HOH551 |
| A | GLY93 |
| A | HOH631 |
| B | ALA98 |
| B | TYR102 |
| A | ASN94 |
| A | LEU95 |
| A | ASP117 |
| A | ILE118 |
| A | ASN119 |
| A | CYS153 |
| A | ILE154 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CAC A 302 |
| Chain | Residue |
| A | ARG17 |
| A | ARG20 |
| A | TYR21 |
| A | HOH584 |
| B | ASN192 |
| B | HIS194 |
| B | HOH411 |
| B | HOH471 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN A 303 |
| Chain | Residue |
| A | HIS194 |
| A | HOH570 |
| B | CAC302 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 304 |
| Chain | Residue |
| A | ASP181 |
| B | GLU24 |
| B | CAC302 |
| B | HOH403 |
| B | HOH592 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 305 |
| Chain | Residue |
| A | GLU24 |
| A | HOH527 |
| A | HOH584 |
| A | HOH585 |
| B | ASP181 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 306 |
| Chain | Residue |
| A | ASP187 |
| A | HOH503 |
| A | HOH557 |
| A | HOH657 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAI B 301 |
| Chain | Residue |
| A | ALA98 |
| A | TYR102 |
| B | ILE90 |
| B | GLY93 |
| B | ASN94 |
| B | LEU95 |
| B | ASP117 |
| B | ILE118 |
| B | LEU122 |
| B | CYS153 |
| B | ILE154 |
| B | PRO155 |
| B | THR162 |
| B | PHE177 |
| B | VAL193 |
| B | LEU195 |
| B | HOH421 |
| B | HOH432 |
| B | HOH448 |
| B | HOH460 |
| B | HOH516 |
| B | HOH542 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CAC B 302 |
| Chain | Residue |
| A | ASN192 |
| A | HIS194 |
| A | ZN303 |
| A | ZN304 |
| A | HOH505 |
| B | ARG20 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 303 |
| Chain | Residue |
| A | HOH527 |
| B | HIS194 |
| B | HOH491 |
| B | HOH492 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 304 |
| Chain | Residue |
| B | GLU136 |
| B | HOH435 |
| B | HOH452 |
| B | HOH453 |
| B | HOH541 |
