Structure of PDB 6rdu Chain Y Binding Site BS02

Receptor Information
>6rdu Chain Y (length=521) Species: 37502 (Polytomella sp. Pringsheim 198.80) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DAGYVSQVIGPVVDVRFDGELPSILSSLEVEGHSVRLVLEVAQHMGDNTV
RCIAMDSTDGLVRGQKVVDTGSPIKVPVGRGTLGRIMNVIGEPVDEQGPI
DAADIWSIHREAPEFTEQSTEQEILVTGIKVVDLLAPYQRGGKIGLFGGA
GVGKTVLIMELINNVAKAHGGFSVFAGVGERTREGNDLYREMIESGVIKL
GAERGNSKCTLVYGQMNEPPGARARVALTGLTVAEYFRDIEGQDVLLFVD
NIFRFTQANSEVSALLGRIPSAVGYQPTLATDLGGLQERITTTTKGSITS
VQAVYVPADDLTDPAPATTFAHLDATTVLSRSIAELGIYPAVDPLDSTSR
MLNPNVIGAEHYNVARGVQKVLQDYKNLQDIIAILGMDELSEEDKLTVAR
ARKIQRFLSQPFQVAEVFTGTPGKYVDLADTISGFQGVLTGKYDDLPEMA
FYMVGDIKEVKEKADKMAKDIASRKEADNKKVSEELKDIPSLDKLVSEIK
EVVIEEDDGLEEDFKAEALSS
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 chain6rdu Chain Y Residue 602 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6rdu Rotary substates of mitochondrial ATP synthase reveal the basis of flexible F 1 -F o coupling.
Resolution3.5 Å
Binding residue
(original residue number in PDB)		T190 E215
Binding residue
(residue number reindexed from 1)		T155 E180
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K189 E215 R216 R385
Catalytic site (residue number reindexed from 1) K154 E180 R181 R350
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase activity
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:0005739 mitochondrion
GO:0016020 membrane
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:6rdu, PDBe:6rdu, PDBj:6rdu
PDBsum6rdu
PubMed31221832
UniProtA0ZW41

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