Structure of PDB 1ii9 Chain A

Receptor sequence
>1ii9A (length=544) Species: 562 (Escherichia coli) [Search protein sequence]
MQFLQNIPPYLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNV
GQVFSQTIGNTIQAIASVPGLSALEIDPQAAAQQYRARIVDPIKGVLPDD
VVSSINEQLSGACTTEIAAFDEFTGLLTDASLLTRFDHIIFDTAPTGHTI
RLLQLPGAWSSFIDSCLGPMAGLEKQREQYAYAVEALSDPKRTRLVLVAR
LQKSTLQEVARTHLELAAIGLKNQYLVINGVLPKTEAANDTLAAAIWERE
QEALANLPADLAGLPTDTLFLQPVNMVGVSALSRLLSTQRPDIPSLSALV
DDIARNEHGLIMLMGKGGVGKTTMAAAIAVRLADMGFDVHLTTSDPAAHL
NNLQVSRIDPHEETERYRQHVLETKGKELDEAGKRLLEEDLRSPCTEEIA
VFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDATTPMMLLQDPERTKVLL
VTLPETTPVLEAANLQADLERAGIHPWGWIINNSLSIADTRSPLLRMRAQ
QELPQIESVKRQHASRVALVPVLASEPTGIDKLKQLAGHHHHHH
3D structure
PDB1ii9 Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation.
ChainA
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K16 G18 G20 K21 T22 S23 D45 A47 T502
Catalytic site (residue number reindexed from 1) K16 G18 G20 K21 T22 S23 D45 A47 T457
Enzyme Commision number 7.3.2.7: arsenite-transporting ATPase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0015446 ATPase-coupled arsenite transmembrane transporter activity
GO:0016887 ATP hydrolysis activity
Biological Process
GO:0046685 response to arsenic-containing substance
GO:0071722 detoxification of arsenic-containing substance

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Molecular Function
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Biological Process
External links
PDB RCSB:1ii9, PDBe:1ii9, PDBj:1ii9
PDBsum1ii9
PubMed11395509
UniProtP08690|ARSA1_ECOLX Arsenical pump-driving ATPase (Gene Name=arsA)

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