Structure of PDB 5lqx Chain E Binding Site BS01

Receptor Information
>5lqx Chain E (length=469) Species: 870730 (Ogataea angusta) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PASGKIRAVIGAVVDVQFEQGELPAILNALTIDQGNNQKLVLEVAQHLGE
NAVRAIAMDGTEGLVRGQTVVDTGAPISVPVGRGTLGRIINVVGEPIDER
GPIECKQRNPIHADPPSFVEQSTEAEVLETGIKVVDLLAPYARGGKIGLF
GGAGVGKTVFIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGV
INLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFVD
NIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGLLQERITTTRKGSVTS
VQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKSR
LLDVSVVGQEHYDVATGVQQTLQAYKSLQDIIAILGMDELSEQDKLTVER
ARKIQRFLSQPFAVAEVFTGIEGKLVRLKDTIASFKAVLEGKYDHLPENA
FYMVGGIEDVVAKAEKIAA
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 chain5lqx Chain E 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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PDB5lqx Structure of the mitochondrial ATP synthase fromPichia angustadetermined by electron cryo-microscopy.
Resolution7.9 Å
Binding residue
(original residue number in PDB)		A160 G161 G163 K164 T165 V166 Y346 A422
Binding residue
(residue number reindexed from 1)		A153 G154 G156 K157 T158 V159 Y339 A415
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) G161 G187 V188 S354
Catalytic site (residue number reindexed from 1) G154 G180 V181 S347
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
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:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
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:5lqx, PDBe:5lqx, PDBj:5lqx
PDBsum5lqx
PubMed27791192
UniProtC0HK52|ATPB_PICAN ATP synthase subunit beta, mitochondrial (Gene Name=ATP2)

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