Structure of PDB 6tmk Chain E2

Receptor sequence
>6tmkE2 (length=507) Species: 507601 (Toxoplasma gondii GT1) [Search protein sequence]
EMSRLLEERIAGWKTQTSTEEVGRVVSVGDGIARLFGLEGVQAGELVEFQ
NGMTGMALNLETDNVGVVIFGDDRSVLEGDSVKRTGRIVDVPIGPGLLGR
VVDALGNPIDGKGPIPAKERRRVELKAPGIIPRKSVHEPMMTGLKCVDAL
VPVGRGQRELIIGDRQTGKTAVAVDAIINQKEINDSTDDESKKLYCIYVA
VGQKRSTVAQIVKALEQRDAMKYTTVVAATASEAAPLQFLAPYSGCAMGE
WFRDSGRHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDVFYLHSRL
LERAAKMGDKSGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETE
LFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGTMKLELAQYREVAAFAQ
FGSDLDASTRQLLTRGTALTELLKQRQYSPMKNSVQVCVLYCGVKGYLDP
LDPKEISRFESLFIDYINANHQDILKTIETEKELSEKTEAKLRAAVDEFV
AMNEFKK
3D structure
PDB6tmk ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria.
ChainE2
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K226 Q260 K261 R425
Catalytic site (residue number reindexed from 1) K169 Q203 K204 R368
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ATP E2 K226 T227 A228 F409 R414 Q484 K169 T170 A171 F352 R357 Q427
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase 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: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:6tmk, PDBe:6tmk, PDBj:6tmk
PDBsum6tmk
PubMed33402698
UniProtS7UU80

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