Structure of PDB 5ik2 Chain J Binding Site BS01

Receptor Information
>5ik2 Chain J (length=468) Species: 986075 (Caldalkalibacillus thermarum TA2.A1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VEVGTVIQVGDGIARVHGLEKVMAGELLEFENGVMGMAQNLEEDNVGVVI
LGPYTEIREGTQVKRTGRIMEVPVGEALLGRVVNPLGQPLDGRGPIETAE
YRPIESPAPGVMDRKSVHEPLQTGIKAIDSMIPIGRGQRELIIGDRQTGK
TTIAIDTIINQKGQDVICIYVAIGQKQSTVAGVVETLRQHDALDYTIVVT
ASASEPAPLLYLAPYAGCAMGEYFMYKGKHALVVYDDLSKQAAAYRELSL
LLRRPPGREAYPGDVFYLHSRLLERAAKLSDEKGGGSLTALPFIETQAGD
VSAYIPTNVISITDGQIFLESDLFYSGVRPAVNVGISVSRVGGAAQIKAM
KKVAGTLRLDLAQYRELQADKATQAKLNRGERTVEILKQDEHKPMPVEEQ
VISIYAVTNGFMDDIPVEDVRRFEEELLSFMRANKDSLLDHIRQTGELPD
TKELDAAIEEFKKGFTPS
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 chain5ik2 Chain J Residue 600 [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)		Q172 G174 K175 T176 T177 F349 R354 E424
Binding residue
(residue number reindexed from 1)		Q147 G149 K150 T151 T152 F324 R329 E391
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q200 K201 R365
Catalytic site (residue number reindexed from 1) K150 Q175 K176 R340
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0032559 adenyl ribonucleotide binding
GO:0043531 ADP binding
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
UniProtF5LA74

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