8H5Z
Crystal structure of RadD/ATP analogue complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0003677 | molecular_function | DNA binding |
A | 0003697 | molecular_function | single-stranded DNA binding |
A | 0004386 | molecular_function | helicase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0006281 | biological_process | DNA repair |
A | 0006301 | biological_process | postreplication repair |
A | 0006302 | biological_process | double-strand break repair |
A | 0006412 | biological_process | translation |
A | 0006974 | biological_process | DNA damage response |
A | 0008270 | molecular_function | zinc ion binding |
A | 0009410 | biological_process | response to xenobiotic stimulus |
A | 0010212 | biological_process | response to ionizing radiation |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0051301 | biological_process | cell division |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003677 | molecular_function | DNA binding |
B | 0003697 | molecular_function | single-stranded DNA binding |
B | 0004386 | molecular_function | helicase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0006281 | biological_process | DNA repair |
B | 0006301 | biological_process | postreplication repair |
B | 0006302 | biological_process | double-strand break repair |
B | 0006412 | biological_process | translation |
B | 0006974 | biological_process | DNA damage response |
B | 0008270 | molecular_function | zinc ion binding |
B | 0009410 | biological_process | response to xenobiotic stimulus |
B | 0010212 | biological_process | response to ionizing radiation |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016887 | molecular_function | ATP hydrolysis activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0051301 | biological_process | cell division |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 290 |
Details | Domain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"31035307","evidenceCode":"ECO:0000303"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 98 |
Details | Region: {"description":"Zinc finger domain","evidences":[{"source":"PubMed","id":"31035307","evidenceCode":"ECO:0000303"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"31035307","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6JDE","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |