Structure of PDB 5fl7 Chain D Binding Site BS01

Receptor Information
>5fl7 Chain D (length=470) Species: 4952 (Yarrowia lipolytica) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GVGSGKIRTVIGAVVDVQFEQDNLPAILNALTIDRGEGNKLVLEVAQHLG
ENTVRTIAMDGTEGLVRGTSVADTGAPITIPVGRGTLGRIINVCGEPIDE
RGPIEATKFLPIHADPPTFAEQSTTAEVLETGIKVVDLLAPYARGGKIGL
FGGAGVGKTVFIQELINNIAKAHGGFSVFCGVGERTREGNDLYREMKETG
VINLEGESKVTLVFGQMNEPPGARARVALTGLTIAEYFRDEEGQDVLLFV
DNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGALQERITTTQKGSVT
SVQAVYVPADDLTDPAPATTFAHLDATTVLSRGISELGIYPAVDPLDSKS
RLLDIDVVGQEHYDVASNVQQTLQAYKSLQDIIAILGMDELSEQDKLTVE
RARKIQRFLSQPFTVAEVFTGIEGRLVSLKDTVRSFKEILDGKHDALPEA
AFYMVGGIEEVVAKAEKLAA
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 chain5fl7 Chain D Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		G191 G193 K194 T195 V196 Y376 F455
Binding residue
(residue number reindexed from 1)		G155 G157 K158 T159 V160 Y340 F419
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K194 E220 R221 R387
Catalytic site (residue number reindexed from 1) K158 E184 R185 R351
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: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: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: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:5fl7, PDBe:5fl7, PDBj:5fl7
PDBsum5fl7
PubMed27373333
UniProtQ6CFT7|ATPB_YARLI ATP synthase subunit beta, mitochondrial (Gene Name=ATP2)

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