Structure of PDB 7yry Chain C Binding Site BS01

Receptor Information
>7yry Chain C (length=489) Species: 1116234 (Acinetobacter baumannii AB5075) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AKNEGTIVMVSDGIVRIHGLADAMYGEMIEFDGGLFGMALNLEQDSVGAV
VLGNYLSLQEGQKARCTGRVLEVPVGPELLGRVVDALGNPIDGKGPIDAK
LTDAVEKVAPGVIWRQSVDQPVQTGYKSVDTMIPVGRGQRELIIGDRQTG
KTAMAIDAIIAQKNSGIKCVYVAIGQKQSTIANVVRKLEETGAMAYTTVV
AAAAADPAAMQYLAPYSGCTMGEYFRDRGEDALIIYDDLSKQAVAYRQIS
LLLRRPPGREAYPGDVFYLHSRLLERASRVSAEYVEKFTNGAVTGKTGSL
TALPIIETQAGDVSAFVPTNVISITDGQIFLETSLFNAGIRPAVNAGISV
SRVGGSAQTKIIKKLSGGIRTALAQYRELAAFAQFASDLDEATRKQLEHG
QRVTELMKQKQYAPYSIADQAVSVYASNEGYMADVEVKKIVDFDAALIAY
FRSEYAPLMKQIDETGDYNKDIEAAIKAGIESFKATQTY
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 chain7yry Chain C Residue 602 [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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PDB7yry Atomic insights of an up and down conformation of the Acinetobacter baumannii F 1 -ATPase subunit epsilon and deciphering the residues critical for ATP hydrolysis inhibition and ATP synthesis.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		R172 Q173 G175 K176 T177 A178 R366 Q436
Binding residue
(residue number reindexed from 1)		R147 Q148 G150 K151 T152 A153 R341 Q411
Annotation score5
Enzymatic activity
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:7yry, PDBe:7yry, PDBj:7yry
PDBsum7yry
PubMed37318822
UniProtA3M142|ATPA_ACIBT ATP synthase subunit alpha (Gene Name=atpA)

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