Structure of PDB 4tsf Chain F Binding Site BS01

Receptor Information
>4tsf Chain F (length=466) Species: 9913 (Bos taurus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTV
RTIAMDGTEGLVRGQKVLDSGAPIRIPVGPETLGRIMNVIGEPIDERGPI
KTKQFAAIHAEAPEFVEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGA
GVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL
KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNI
FRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQ
AIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIM
DPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR
KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYDHLPEQAFY
MVGPIEEAVAKADKLA
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 chain4tsf Chain C 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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PDB4tsf Pathway of binding of the intrinsically disordered mitochondrial inhibitor protein to F1-ATPase.
Resolution3.2 Å
Binding residue
(original residue number in PDB)		R356 D359
Binding residue
(residue number reindexed from 1)		R348 D351
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) K162 E188 R189 R356
Catalytic site (residue number reindexed from 1) K154 E180 R181 R348
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: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:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner 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:4tsf, PDBe:4tsf, PDBj:4tsf
PDBsum4tsf
PubMed25049402
UniProtP00829|ATPB_BOVIN ATP synthase subunit beta, mitochondrial (Gene Name=ATP5F1B)

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