Structure of PDB 6qum Chain A Binding Site BS01

Receptor Information
>6qum Chain A (length=578) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIQGVIQKIAGPAVIAKGMLGARMYDICKVGEEGLVGEIIRLDGDTAFVQ
VYEDTSGLKVGEPVVSTGLPLAVELGPGMLNGIYDGIQRPLERIREKTGI
YITRGVVVHALDREKKWAWTPMVKPGDEVRGGMVLGTVPEFGFTHKILVP
PDVRGRVKEVKPAGEYTVEEPVVVLEDGTELKMYHTWPVRRARPVQRKLD
PNTPFLTGMRILDVLFPVAMGGTAAIPGPFGSGKTVTQQSLAKWSNADVV
VYVGCGERGNEMTDVLVEFPELTDPKTGGPLMHRTVLIANTSNMPVAARE
ASIYVGVTIAEYFRDQGFSVALMADSTSRWAEALREISSRLEEMPAEEGY
PPYLAARLAAFYERAGKVITLGGEEGAVTIVGAVSPPGGDMSEPVTQSTL
RIVGAFWRLDASLAFRRHFPAINWNGSYSLFTSALDPWYRENVAEDYPEL
RDAISELLQREAGLQEIVQLVGPDALQDAERLVIEVGRIIREDFLQQNAY
HEVDAYCSMKKAYGIMKMILAFYKEAEAAIKRGVSIDEILQLPVLERIGR
ARYVSEEEFPAYFEEAMKEIQGAFKALA
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 chain6qum Chain A Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6qum Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase.
Resolution3.25 Å
Binding residue
(original residue number in PDB)		T235 E257 E261
Binding residue
(residue number reindexed from 1)		T235 E257 E261
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K234 E257 R258 L430
Catalytic site (residue number reindexed from 1) K234 E257 R258 L430
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: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
Cellular Component
GO:0045259 proton-transporting ATP synthase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6qum, PDBe:6qum, PDBj:6qum
PDBsum6qum
PubMed31439765
UniProtQ56403|VATA_THET8 V-type ATP synthase alpha chain (Gene Name=atpA)

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