Structure of PDB 1ii0 Chain B

Receptor sequence
>1ii0B (length=553) Species: 562 (Escherichia coli) [Search protein sequence]
MQFLQNIPPYLFFTGKGGVGKTSISCATAIRLAEQGKRVLLVSTDPASNV
GQVFSQTIGNTIQAIASVPGLSALEIDPQAAAQQYRARIVDPIKGVLPDD
VVSSINEQLSGACTTEIAAFDEFTGLLTDASLLTRFDHIIFDTAPTGHTI
RLLQLPGAWSSFIDSNPEGASCLGPMAGLEKQREQYAYAVEALSDPKRTR
LVLVARLQKSTLQEVARTHLELAAIGLKNQYLVINGVLPKTEAANDTLAA
AIWEREQEALANLPADLAGLPTDTLFLQPVNMVGVSALSRLLSTQPQQRP
DIPSLSALVDDIARNEHGLIMLMGKGGVGKTTMAAAIAVRLADMGFDVHL
TTSDPAALNNLQVSRIDPHEETERYRQHVLETKGKELDEAGKRLLEEDLR
SPCTEEIAVFQAFSRVIREAGKRFVVMDTAPTGHTLLLLDATTTPMMLLQ
DPERTKVLLVTLPETTPVLEAANLQADLERAGIHPWGWIINNSLSIADTR
SPLLRMRAQQELPQIESVKRQHASRVALVPVLASEPTGIDKLKQLAGHHH
HHH
3D structure
PDB1ii0 Conformational changes in four regions of the Escherichia coli ArsA ATPase link ATP hydrolysis to ion translocation.
ChainB
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K1016 G1018 G1020 K1021 T1022 S1023 D1045 A1047 T1502
Catalytic site (residue number reindexed from 1) K16 G18 G20 K21 T22 S23 D45 A47 T466
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:1ii0, PDBe:1ii0, PDBj:1ii0
PDBsum1ii0
PubMed11395509
UniProtP08690|ARSA1_ECOLX Arsenical pump-driving ATPase (Gene Name=arsA)

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