Structure of PDB 6ynz Chain A2 Binding Site BS01

Receptor Information
>6ynz Chain A2 (length=512) Species: 5911 (Tetrahymena thermophila) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LSTGEASVVLAEKIKGITQQNDITEYGTVISIGDGIARVFGLTKVQAGEM
VEFKSGIRGMALNLETDNVGVVVLGNDRDIKEGDVVKRTGAIVDVPIGEA
MCGRVFDALGNPIDGLGPLKTTQRARVEIKAPGIIPRQSVRQPMQTGIKC
VDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKEAFNTGDVKKQLYCI
YVAVGQKRSTIANLVSILKQHDCMKFTIVVCATASDAAPLQFLAPYSGCA
IGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLH
SRLLERAAKMNDSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL
ETELFYKGIRPAINVGLSVSRVGSAAQIKAMKKIAGNLKLTLATYRELAA
FSQFGSDLDAKTQQQLNTGERLVEMLKQNQYTPMKVEEQVCIIFAGVKGF
LDALVTSEVLKFEKKFLEHVRTNHSALLKRIRDSGDLSEVDTNELNTIIP
LFIQEGGFKLKA
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 chain6ynz Chain D2 Residue 501 [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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PDB6ynz Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		S403 R404
Binding residue
(residue number reindexed from 1)		S370 R371
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K206 Q239 K240 R404
Catalytic site (residue number reindexed from 1) K173 Q206 K207 R371
Enzyme Commision number ?
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
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:0016020 membrane
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:6ynz, PDBe:6ynz, PDBj:6ynz
PDBsum6ynz
PubMed33093501
UniProtQ24HY8

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