Structure of PDB 3oee Chain S Binding Site BS02

Receptor Information
>3oee Chain S (length=477) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIV
LFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAA
GRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTG
KTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHD
AMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQ
AVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTAL
PVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRV
GSAAQVKALKQVAGSLKLFLAQYREVAASAQASTKQTLVRGERLTQLLKQ
NQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELL
TEIREKGELSKELLASLKSATESFVAT
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 chain3oee Chain S Residue 700 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3oee Structure of four mutant forms of yeast F1 ATPase: alpha-F405S
Resolution2.74 Å
Binding residue
(original residue number in PDB)		T178 D271
Binding residue
(residue number reindexed from 1)		T152 D245
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K177 Q210 K211 R375
Catalytic site (residue number reindexed from 1) K151 Q184 K185 R349
Enzyme Commision number 3.6.3.14: Transferred entry: 7.1.2.2.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0032559 adenyl ribonucleotide binding
GO:0043531 ADP binding
GO:0046933 proton-transporting ATP synthase activity, rotational mechanism
Biological Process
GO:0006754 ATP biosynthetic process
GO:0015986 proton motive force-driven ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
GO:0005758 mitochondrial intermembrane space
GO:0005829 cytosol
GO:0016020 membrane
GO:0042645 mitochondrial nucleoid
GO:0045261 proton-transporting ATP synthase complex, catalytic core F(1)
GO:0045267 proton-transporting ATP synthase, catalytic core

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3oee, PDBe:3oee, PDBj:3oee
PDBsum3oee
PubMed
UniProtP07251|ATPA_YEAST ATP synthase subunit alpha, mitochondrial (Gene Name=ATP1)

[Back to BioLiP]