Structure of PDB 6oqu Chain B Binding Site BS01

Receptor Information
>6oqu Chain B (length=513) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MQLNSTEISELIKQRIAQFNVVSEAHNEGTIVSVSDGVIRIHGLADCMQG
EMISLPGNRYAIALNLERDSVGAVVMGPYADLAEGMKVKCTGRILEVPVG
RGLLGRVVNTLGAPIDGKGPLDHDGFSAVEAIAPGVIERQSVDQPVQTGY
KAVDSMIPIGRGQRELIIGDRQTGKTALAIDAIINQRDSGIKCIYVAIGQ
KASTISNVVRKLEEHGALANTIVVVATASESAALQYLAPYAGCAMGEYFR
DRGEDALIIYDDLSKQAVAYRQISLLLRRPPGREAFPGDVFYLHSRLLER
AARVNAEYVEAFTKGEVKGKTGSLTALPIIETQAGDVSAFVPTNVISITD
GQIFLETNLFNAGIRPAVNPGISVSRVGGAAQTKIMKKLSGGIRTALAQY
RELAAFSQFASDLDDATRKQLDHGQKVTELLKQKQYAPMSVAQQSLVLFA
AERGYLADVELSKIGSFEAALLAYVDRDHAPLMQEINQTGGYNDEIEGKL
KGILDSFKATQSW
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 chain6oqu Chain B Residue 600 [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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PDB6oqu Cryo-EM structures provide insight into how E. coli F1FoATP synthase accommodates symmetry mismatch.
Resolution3.2 Å
Binding residue
(original residue number in PDB)		Q172 G174 K175 T176 A177 R365 Q433 Q435
Binding residue
(residue number reindexed from 1)		Q172 G174 K175 T176 A177 R365 Q433 Q435
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K175 Q200 K201 R376
Catalytic site (residue number reindexed from 1) K175 Q200 K201 R376
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:0042777 proton motive force-driven plasma membrane ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005886 plasma membrane
GO:0016020 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:6oqu, PDBe:6oqu, PDBj:6oqu
PDBsum6oqu
PubMed32457314
UniProtP0ABB0|ATPA_ECOLI ATP synthase subunit alpha (Gene Name=atpA)

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