7EGT
The crystal structure of the C-terminal domain of T. thermophilus UvrD complexed with the N-terminal domain of UvrB
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003677 | molecular_function | DNA binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006289 | biological_process | nucleotide-excision repair |
| A | 0009380 | cellular_component | excinuclease repair complex |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0003677 | molecular_function | DNA binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006289 | biological_process | nucleotide-excision repair |
| C | 0009380 | cellular_component | excinuclease repair complex |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 770 |
| Details | Domain: {"description":"Helicase ATP-binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 46 |
| Details | Motif: {"description":"Beta-hairpin"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






