Structure of PDB 5hkk Chain E Binding Site BS01

Receptor Information
>5hkk Chain E (length=461) Species: 986075 (Caldalkalibacillus thermarum TA2.A1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NKGRIIQVMGPVVDIQFESGQLPDIYNAITIERPQGGTLTVEAAVHLGDN
VVRCVAMASTDGLVRGLEAVDTGAPISVPVGKATLGRVFNVLGEPIDEQG
EVNAEERHPIHRPAPEFEELSTADEILETGIKVIDLLAPYAKGGKIGLFG
GAGVGKTVLIQELINNVAQEHGGLSVFAGVGERTREGNDLYHEMKDSGVI
SKTSMVFGQMNEPPGARLRVALTGLTMAEYFRDREGQDVLLFIDNIFRFT
QAGSEVSALLGRMPSAVGYQPTLATEMGQLQERITSTKKGSITSIQAIYV
PADDYTDPAPATTFAHLDATTNLERKLAEMGIYPAVDPLASTSRILSPAV
VGEEHYRVARGVQQVLQRYNDLQDIIAILGMDELSDEDKLIVARARKIQR
FLSQPFHVAEQFTGMPGKYVPVKETVRGFKEILEGKHDNLPEEAFYMVGT
IDEAVEKAKKL
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain5hkk Chain E Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5hkk Regulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarum.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		G156 K157 T158 V159 Y334
Binding residue
(residue number reindexed from 1)		G155 K156 T157 V158 Y333
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K157 E183 R184 R345
Catalytic site (residue number reindexed from 1) K156 E182 R183 R344
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:5hkk, PDBe:5hkk, PDBj:5hkk
PDBsum5hkk
PubMed27621435
UniProtF5LA72

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