2DT5
Crystal Structure of TTHA1657 (AT-rich DNA-binding protein) from Thermus thermophilus HB8
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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 401 |
| Chain | Residue |
| A | SER30 |
| A | SER31 |
| A | ARG58 |
| A | GLY61 |
| A | HOH629 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 402 |
| Chain | Residue |
| B | THR57 |
| B | GLY59 |
| B | VAL60 |
| B | GLY61 |
| B | SER30 |
| B | SER31 |
| B | ARG46 |
| B | TYR55 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 403 |
| Chain | Residue |
| A | ARG72 |
| A | ASN78 |
| A | HOH690 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 404 |
| Chain | Residue |
| B | ARG120 |
| B | ARG123 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 405 |
| Chain | Residue |
| A | TYR98 |
| A | PRO99 |
| A | GLY100 |
| A | PHE101 |
| A | GLY102 |
| A | HOH723 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 406 |
| Chain | Residue |
| A | LYS155 |
| A | LEU159 |
| A | HOH676 |
| A | HOH683 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE NAD A 301 |
| Chain | Residue |
| A | GLY87 |
| A | MET88 |
| A | GLY89 |
| A | ARG90 |
| A | LEU91 |
| A | ASP112 |
| A | VAL113 |
| A | ASP114 |
| A | LYS117 |
| A | THR147 |
| A | VAL148 |
| A | PRO149 |
| A | ARG150 |
| A | GLU151 |
| A | PHE171 |
| A | ALA172 |
| A | PRO173 |
| A | VAL187 |
| A | PHE189 |
| A | HOH602 |
| A | HOH604 |
| A | HOH613 |
| A | HOH614 |
| A | HOH686 |
| A | HOH687 |
| A | HOH720 |
| B | ALA94 |
| B | LEU95 |
| B | TYR98 |
| B | PRO99 |
| B | PHE189 |
| B | HOH461 |
| site_id | AC8 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE NAD B 302 |
| Chain | Residue |
| A | ALA94 |
| A | LEU95 |
| A | TYR98 |
| A | HOH612 |
| B | VAL86 |
| B | GLY87 |
| B | GLY89 |
| B | ARG90 |
| B | LEU91 |
| B | ASP112 |
| B | VAL113 |
| B | ASP114 |
| B | LYS117 |
| B | THR147 |
| B | VAL148 |
| B | PRO149 |
| B | ARG150 |
| B | ALA152 |
| B | PHE171 |
| B | ALA172 |
| B | PRO173 |
| B | VAL187 |
| B | PHE189 |
| B | HOH407 |
| B | HOH411 |
| B | HOH446 |
| B | HOH447 |
| B | HOH449 |
| B | HOH464 |
| B | HOH490 |
| B | HOH498 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 601 |
| Chain | Residue |
| A | GLY25 |
| A | VAL26 |
| A | HIS27 |
| A | ARG28 |
| A | HOH738 |
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 |
