Structure of PDB 5fl7 Chain B Binding Site BS01

Receptor Information
>5fl7 Chain B (length=479) Species: 4952 (Yarrowia lipolytica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ANLNETGRVLSVGDGIARVFGLNNIQAEELVEFASGVKGMALNLEAGQVG
IVLFGSDRLVKEGETVKRSGSIVDVPVGPALLGRVVDALGNPIDGKGPIE
TEFRIRAQVKAPGILPRTSVNEPMQTGLKAVDALVPIGRGQRELIIGDRQ
TGKTQIAIDTILNQKRWNYGQDEKKKLYCVYVAVGQKRSTVAQLVQTLEH
HDALKYSIIVAATASEAAPLQYLAPFTGTAMGEWFRDNGKGALIVFDDLS
KQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNEREGGGSLT
ALPIIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVS
RVGSAAQVKAMKQVAGSLKLFLAQYREVAADLDASTKQTLTRGERLTLLL
KQKQASPMSSEEMVPLIYAGVNGYIDNIPVKQVEKFEAEFVSYLHANESD
LLKDIAATGELSKENLEKLKSITENFVGS
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 chain5fl7 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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PDB5fl7 Structure of a Complete ATP Synthase Dimer Reveals the Molecular Basis of Inner Mitochondrial Membrane Morphology.
Resolution3.5 Å
Binding residue
(original residue number in PDB)		Q198 G200 K201 T202 Q203 F383 P389 Q456
Binding residue
(residue number reindexed from 1)		Q150 G152 K153 T154 Q155 F335 P341 Q402
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K201 Q234 K235 R399
Catalytic site (residue number reindexed from 1) K153 Q186 K187 R351
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:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0016020 membrane
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)
GO:0045267 proton-transporting ATP synthase, catalytic core

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5fl7, PDBe:5fl7, PDBj:5fl7
PDBsum5fl7
PubMed27373333
UniProtQ6C326|ATPA_YARLI ATP synthase subunit alpha, mitochondrial (Gene Name=ATP1)

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