Structure of PDB 5bn3 Chain A Binding Site BS02

Receptor Information
>5bn3 Chain A (length=563) Species: 228908 (Nanoarchaeum equitans Kin4-M) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MNRIISINGPLVIAKGKFSIFEVVRVGEEKLIGEVIGIENDKAYIQVYED
TNGLKVGEPVFNTGKPLTIELGPGLLANIFDGLGRPLKDIYEKTQSIYIP
KGIDLPTLDRKKVWEFIPKKKKGDTIKGGDIIGTVNENGFEHRIIVPPNV
EGKIEEIYEGNFTIEETIAIVNGKPIKLYHEWPIRKPRPYKEKLDYNYPF
ITGTRVLDIMFPIAKGGSAAVPGPFGSGKTVLNQQIAKWADSDIVIYIGC
GERGNEMTEVLEEFPKLKDPKTGKPLMYRTILIANTSNMPIAAREASIYL
GATIGEYFRDQGYSVVVNADSTSRWAEALREISSRLGEIPSEEGYPAYLL
RKLAEFYERSGRVRTLNDLEGSLTIIGAVSPPGGDFSEPVTQNTLRLVGA
LWALDSKLAYKRHYPAINYLISYTKQWEFVKKYFEELYEDVIEIREEFFA
ILKRESELMDIVSIVGALSDNEKIYLHMGRIIREGFLQQDAFDENDSYSP
LEKTIELMRIIHKYYVTVKQLLGIPLEEIEQKGIHEKIIKLRYKSLKEFR
EEIKAIEQEILSL
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 chain5bn3 Chain A Residue 610 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5bn3 Structural Basis for a Unique ATP Synthase Core Complex from Nanoarcheaum equitans
Resolution2.0 Å
Binding residue
(original residue number in PDB)		V315 S372 T374
Binding residue
(residue number reindexed from 1)		V315 S372 T374
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K229 E252 R253 K425
Catalytic site (residue number reindexed from 1) K229 E252 R253 K425
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
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:0042777 proton motive force-driven plasma membrane ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport

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Molecular Function
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Biological Process
External links
PDB RCSB:5bn3, PDBe:5bn3, PDBj:5bn3
PDBsum5bn3
PubMed26370083
UniProtQ74MJ7|VATA_NANEQ V-type ATP synthase alpha chain (Gene Name=atpA)

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