Structure of PDB 2vsf Chain A

Receptor sequence
>2vsfA (length=588) Species: 2303 (Thermoplasma acidophilum) [Search protein sequence]
YGVALESPTGSGKTIMALKSALQYSSERKLKVLYLVRTNSQEEQVIKELR
SLSSTMKIRAIPMQGRVNMCILYRMVDDLHEINAESLAKFCNMKKREVMA
GNEAACPYFNFKIRSDETKRFLFDELPTAEEFYDYGERNNVCPYESMKAA
LPDADIVIAPYAYFLNRSVAEKFLSHWGVSRNQIVIILDEAHNLPDIGRS
IGSFRISVESLNRADREAQAYGDPELSQKIHVSDLIEMIRSALQSMVSER
CGKGDVRIRFQEFMEYMRIMNKRSEREIRSLLNYLYLFGEYVENEKEKVG
KVPFSYCSSVASRIIAFSDQDEEKYAAILSPEDGGYMQAACLDPSGILEV
LKESKTIHMSGTLDPFDFYSDITGFEIPFKKIGEIFPPENRYIAYYDGVS
SKYDTLDEKELDRMATVIEDIILKVKKNTIVYFPSYSLMDRVENRVSFEH
MKEYRGIDQKELYSMLKKFRRDHGTIFAVSGGRLSEGNELEMIILAGLPF
PRPDAINRSLFDYYERKYGKGWEYSVVYPTAIKIRQEIGRLIRSAEDTGA
CVILDKRAGQFRKFIPDMKKTSDPASDIYNFFISAQAR
3D structure
PDB2vsf Crystal Structure of the Fes Cluster-Containing Nucleotide Excision Repair Helicase Xpd.
ChainA
Resolution2.9 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 SF4 A R88 C92 L94 C113 C128 F131 C164 R66 C70 L72 C91 C106 F109 C142
BS02 CA A E312 E315 E290 E293
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0003677 DNA binding
GO:0003678 DNA helicase activity
GO:0004386 helicase activity
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016818 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
GO:0016853 isomerase activity
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
GO:0051539 4 iron, 4 sulfur cluster binding
Biological Process
GO:0006139 nucleobase-containing compound metabolic process
GO:0006281 DNA repair
GO:0032508 DNA duplex unwinding

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Molecular Function
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Biological Process
External links
PDB RCSB:2vsf, PDBe:2vsf, PDBj:2vsf
PDBsum2vsf
PubMed18578568
UniProtQ9HM14|XPD_THEAC ATP-dependent DNA helicase XPD (Gene Name=Ta0057)

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