Structure of PDB 8h9v Chain F Binding Site BS02

Receptor Information
>8h9v Chain F (length=466) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLEVAQHLGESTV
RTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPI
KTKQFAPIHAEAPEFMEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGA
GVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL
KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNI
FRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQ
AIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIM
DPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR
KIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFY
MVGPIEEAVAKADKLA
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain8h9v Chain F Residue 502 [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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PDB8h9v Structure of the human ATP synthase.
Resolution3.02 Å
Binding residue
(original residue number in PDB)		E191 D259
Binding residue
(residue number reindexed from 1)		E180 D248
Annotation score1
Enzymatic activity
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:0042288 MHC class I protein binding
GO:0043532 angiostatin binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
GO:0046961 proton-transporting ATPase activity, rotational mechanism
Biological Process
GO:0001525 angiogenesis
GO:0001649 osteoblast differentiation
GO:0006091 generation of precursor metabolites and energy
GO:0006629 lipid metabolic process
GO:0006754 ATP biosynthetic process
GO:0006933 negative regulation of cell adhesion involved in substrate-bound cell migration
GO:0015986 proton motive force-driven ATP synthesis
GO:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0043536 positive regulation of blood vessel endothelial cell migration
GO:0046034 ATP metabolic process
GO:0051453 regulation of intracellular pH
GO:0098761 cellular response to interleukin-7
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005759 mitochondrial matrix
GO:0005886 plasma membrane
GO:0009986 cell surface
GO:0016020 membrane
GO:0016469 proton-transporting two-sector ATPase complex
GO:0031090 organelle membrane
GO:0031966 mitochondrial membrane
GO:0042645 mitochondrial nucleoid
GO:0045259 proton-transporting ATP synthase complex
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)
GO:0045267 proton-transporting ATP synthase, catalytic core
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8h9v, PDBe:8h9v, PDBj:8h9v
PDBsum8h9v
PubMed37244256
UniProtP06576|ATPB_HUMAN ATP synthase subunit beta, mitochondrial (Gene Name=ATP5F1B)

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