Structure of PDB 5ik2 Chain E Binding Site BS02

Receptor Information
>5ik2 Chain E (length=462) Species: 986075 (Caldalkalibacillus thermarum TA2.A1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNKGRIIQVMGPVVDIQFESGQLPDIYNAITIERPQGGTLTVEAAVHLGD
NVVRCVAMASTDGLVRGLEAVDTGAPISVPVGKATLGRVFNVLGEPIDEQ
GEVNAEERHPIHRPAPEFEELSTADEILETGIKVIDLLAPYAKGGKIGLF
GGAGVGKTVLIQELINNVAQEHGGLSVFAGVGERTREGNDLYHEMKDSGV
ISKTSMVFGQMNEPPGARLRVALTGLTMAEYFRDREGQDVLLFIDNIFRF
TQAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSITSIQAIY
VPADDYTDPAPATTFAHLDATTNLERKLAEMGIYPAVDPLASTSRILSPA
VVGEEHYRVARGVQQVLQRYNDLQDIIAILGMDELSDEDKLIVARARKIQ
RFLSQPFHVAEQFTGMPGKYVPVKETVRGFKEILEGKHDNLPEEAFYMVG
TIDEAVEKAKKL
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain5ik2 Chain E Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5ik2 Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.
Resolution2.6 Å
Binding residue
(original residue number in PDB)		D245 R249
Binding residue
(residue number reindexed from 1)		D245 R249
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K157 E183 R184 R345
Catalytic site (residue number reindexed from 1) K157 E183 R184 R345
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0046872 metal ion binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0045259 proton-transporting ATP synthase complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ik2, PDBe:5ik2, PDBj:5ik2
PDBsum5ik2
PubMed27621435
UniProtF5LA72

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