Structure of PDB 2r9v Chain A Binding Site BS01

Receptor Information
>2r9v Chain A (length=487) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KSFEEKIDLEDTGKVIQVGDGIARAYGLNKVMVSELVEFVETGVKGVAFN
LEEDNVGIIILGEYKDIKEGHTVRRLKRIIEVPVGEELLGRVVNPLGEPL
DGKGPINAKNFRPIEIKAPGVIYRKPVDTPLQTGIKAIDSMIPIGRGQRE
LIIGDRQTGKTAIAIDTIINQKGQGVYCIYVAIGQKKSAIARIIDKLRQY
GAMEYTTVVVASASDPASLQYIAPYAGCAMGEYFAYSGRDALVVYDDLSK
HAVAYRQLSLLMRRPPGREAYPGDIFYLHSRLLERAVRLNDKLGGGSLTA
LPIVETQANDISAYIPTNVISITDGQIYLEPGLFYAGQRPAINVGLSVSR
VGGSAQIKAMKQVAGMLRIDLAQYRELETFAQFATELDPATRAQIIRGQR
LMELLKQEQYSPMPVEEQVVVLFAGVRGYLDDLPVEEVRRFEKEFLRFMH
EKHQDILDDIKTKKELTSETEEKLKKAIEEFKTTFRV
Ligand information
Ligand IDATP
InChIInChI=1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyZKHQWZAMYRWXGA-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=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[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@](O)(=O)O[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
FormulaC10 H16 N5 O13 P3
NameADENOSINE-5'-TRIPHOSPHATE
ChEMBLCHEMBL14249
DrugBankDB00171
ZINCZINC000004261765
PDB chain2r9v Chain A Residue 506 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2r9v Crystal structure of ATP synthase subunit alpha (TM1612) from Thermotoga maritima at 2.10 A resolution
Resolution2.1 Å
Binding residue
(original residue number in PDB)		R172 Q173 G175 K176 T177 A178 F350 R355 Q423 Q425
Binding residue
(residue number reindexed from 1)		R156 Q157 G159 K160 T161 A162 F334 R339 Q407 Q409
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K176 Q201 K202 R366
Catalytic site (residue number reindexed from 1) K160 Q185 K186 R350
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: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:2r9v, PDBe:2r9v, PDBj:2r9v
PDBsum2r9v
PubMed
UniProtQ9X1U7|ATPA_THEMA ATP synthase subunit alpha (Gene Name=atpA)

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