3KEO
Crystal Structure of a Rex-family transcriptional regulatory protein from Streptococcus agalactiae complexed with NAD+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0051775 | biological_process | response to redox state |
| 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 | 0051775 | biological_process | response to redox state |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE NAD A 213 |
| Chain | Residue |
| A | GLY91 |
| A | THR155 |
| A | VAL156 |
| A | PRO157 |
| A | SER158 |
| A | VAL164 |
| A | PHE179 |
| A | SER180 |
| A | PRO181 |
| A | LEU197 |
| A | HOH225 |
| A | CYS92 |
| A | HOH235 |
| A | HOH309 |
| A | HOH371 |
| A | HOH374 |
| A | HOH396 |
| A | HOH402 |
| A | HOH423 |
| B | ALA98 |
| B | LEU99 |
| B | TYR102 |
| A | GLY93 |
| A | ASN94 |
| A | ILE95 |
| A | ASP117 |
| A | LEU118 |
| A | ASN121 |
| A | ILE137 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 214 |
| Chain | Residue |
| A | TYR102 |
| A | ARG103 |
| B | NAD213 |
| B | HOH414 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 215 |
| Chain | Residue |
| A | ARG14 |
| A | HOH336 |
| B | ARG14 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 216 |
| Chain | Residue |
| A | GLU77 |
| A | ARG212 |
| A | HOH512 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 217 |
| Chain | Residue |
| A | HIS105 |
| A | ASP106 |
| A | HOH331 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 218 |
| Chain | Residue |
| A | ARG14 |
| B | HOH218 |
| B | HOH378 |
| site_id | AC7 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 213 |
| Chain | Residue |
| A | ALA98 |
| A | LEU99 |
| A | TYR102 |
| A | MG214 |
| B | GLY91 |
| B | CYS92 |
| B | GLY93 |
| B | ASN94 |
| B | ILE95 |
| B | ASP117 |
| B | LEU118 |
| B | ILE137 |
| B | THR155 |
| B | VAL156 |
| B | PRO157 |
| B | SER158 |
| B | VAL164 |
| B | PHE179 |
| B | SER180 |
| B | PRO181 |
| B | LEU197 |
| B | HOH227 |
| B | HOH269 |
| B | HOH324 |
| B | HOH333 |
| B | HOH337 |
| B | HOH382 |
| B | HOH390 |
| B | HOH392 |
| B | HOH399 |
| B | HOH414 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 214 |
| Chain | Residue |
| A | GLN202 |
| B | ASP81 |
| B | HIS105 |
| B | MET110 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 215 |
| Chain | Residue |
| A | LEU42 |
| A | GLY43 |
| A | HOH355 |
| B | LYS13 |
| B | HOH288 |
| B | HOH411 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 216 |
| Chain | Residue |
| B | ASP119 |
| B | SER120 |
| B | HOH344 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 78 |
| Details | DNA binding: {"description":"H-T-H motif","evidences":[{"source":"HAMAP-Rule","id":"MF_01131","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01131","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
