Structure of PDB 6jde Chain A

Receptor sequence
>6jdeA (length=560) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
FTLRPYQQEAVDATLNHFRRHKTPAVIVLPTGAGKSLVIAELARLARGRV
LVLAHVKELVAQNHAKYQALGLEADIFAAGHGKVVFGSVQSVARNLDAFQ
GEFSLLIVDECHRIGDDEESQYQQILTHLTKVNPHLRLLGLTATPFRLGK
GWIYQFHYHGMVRGDEKALFRDCIYELPLRYMIKHGYLTPPERLDMPVVQ
YDFSRLQAQSNGLFSEADLNRELKKQQRITPHIISQIMEFAATRKGVMIF
AATVEHAKEIVGLLPAEDAALITGDTPGAERDVLIENFKAQRFRYLVNVA
VLTTGFDAPHVDLIAILRPTESVSLYQQIVGRGLRLAPGKTDCLILDYAG
NPHDLYAPEVGTPKGKSDNVPVQVFCPACGFANTFWGKTTADGTLIEHFG
RRCQGWFEDDDGHREQCDFRFRFKNPQCNAENDAARCDTVLVDPDDMLKA
ALRLKDALVLRCSGMSLQHGHDEKGEWLKITYYDEDGADVSERFRLQTPA
QRTAFEQLFIRPHTRTPGIPLRWITAADILAQQALLRHPDFVVARMKGQY
WQVREKVFDY
3D structure
PDB6jde Crystal structure of a novel ATPase RadD from Escherichia coli.
ChainA
Resolution2.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.6.4.12: DNA helicase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ZN A C384 C387 C411 C425 C376 C379 C403 C417
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003697 single-stranded DNA binding
GO:0004386 helicase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
Biological Process
GO:0006281 DNA repair
GO:0006301 postreplication repair
GO:0006302 double-strand break repair
GO:0006412 translation
GO:0009410 response to xenobiotic stimulus
GO:0010212 response to ionizing radiation
GO:0051301 cell division

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Molecular Function
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Biological Process
External links
PDB RCSB:6jde, PDBe:6jde, PDBj:6jde
PDBsum6jde
PubMed31035307
UniProtP33919|RADD_ECOLI Putative DNA repair helicase RadD (Gene Name=radD)

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