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8H5Y

Crystal structure of RadD- ADP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003697molecular_functionsingle-stranded DNA binding
A0004386molecular_functionhelicase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0006281biological_processDNA repair
A0006301biological_processpostreplication repair
A0006302biological_processdouble-strand break repair
A0006412biological_processtranslation
A0008270molecular_functionzinc ion binding
A0009410biological_processresponse to xenobiotic stimulus
A0010212biological_processresponse to ionizing radiation
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0046872molecular_functionmetal ion binding
A0051301biological_processcell division
B0003677molecular_functionDNA binding
B0003697molecular_functionsingle-stranded DNA binding
B0004386molecular_functionhelicase activity
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0006281biological_processDNA repair
B0006301biological_processpostreplication repair
B0006302biological_processdouble-strand break repair
B0006412biological_processtranslation
B0008270molecular_functionzinc ion binding
B0009410biological_processresponse to xenobiotic stimulus
B0010212biological_processresponse to ionizing radiation
B0016787molecular_functionhydrolase activity
B0016887molecular_functionATP hydrolysis activity
B0046872molecular_functionmetal ion binding
B0051301biological_processcell division
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:31035307, ECO:0007744|PDB:6JDE
ChainResidueDetails
BCYS384
BCYS387
BCYS411
BCYS425
ACYS384
ACYS387
ACYS411
ACYS425

222926

PDB entries from 2024-07-24

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