Structure of PDB 1cow Chain F Binding Site BS02

Receptor Information
>1cow 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 IDAUR
InChIInChI=1S/C25H32O8/c1-7-20-24(4)23(30-16(3)26)25(5,33-20)22(28)18(32-24)13-11-9-8-10-12-17-15(2)19(29-6)14-21(27)31-17/h8-14,18,20,22-23,28H,7H2,1-6H3/b9-8+,12-10+,13-11+/t18-,20+,22-,23+,24-,25-/m0/s1
InChIKeyQXCOFYWOWZJFEA-YJMRODJJSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC[C@@H]1[C@]2([C@H]([C@@](O1)([C@H]([C@@H](O2)\C=C\C=C\C=C\C3=C(C(=CC(=O)O3)OC)C)O)C)OC(=O)C)C
CACTVS 3.341CC[C@H]1O[C@@]2(C)[C@@H](O)[C@@H](O[C@]1(C)[C@H]2OC(C)=O)\C=C\C=C\C=C\C3=C(C)C(=CC(=O)O3)OC
OpenEye OEToolkits 1.5.0CCC1C2(C(C(O1)(C(C(O2)C=CC=CC=CC3=C(C(=CC(=O)O3)OC)C)O)C)OC(=O)C)C
CACTVS 3.341CC[CH]1O[C]2(C)[CH](O)[CH](O[C]1(C)[CH]2OC(C)=O)C=CC=CC=CC3=C(C)C(=CC(=O)O3)OC
ACDLabs 10.04O=C1OC(=C(C(OC)=C1)C)\C=C\C=C\C=C\C3OC2(C(OC(=O)C)C(OC2CC)(C3O)C)C
FormulaC25 H32 O8
NameAUROVERTIN B
ChEMBL
DrugBankDB07394
ZINCZINC000028539463
PDB chain1cow Chain F Residue 602 [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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PDB1cow The structure of bovine F1-ATPase complexed with the antibiotic inhibitor aurovertin B.
Resolution3.1 Å
Binding residue
(original residue number in PDB)		I339 L342 I344 P350 L378 Q385 Q411 R412 Q455 Y458
Binding residue
(residue number reindexed from 1)		I331 L334 I336 P342 L370 Q377 Q403 R404 Q447 Y450
Annotation score1
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
View graph for
Cellular Component
External links
PDB RCSB:1cow, PDBe:1cow, PDBj:1cow
PDBsum1cow
PubMed8692918
UniProtP00829|ATPB_BOVIN ATP synthase subunit beta, mitochondrial (Gene Name=ATP5F1B)

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