Structure of PDB 6tmh Chain A

Receptor sequence
>6tmhA (length=512) Species: 507601 (Toxoplasma gondii GT1) [Search protein sequence]
KISPSEMSRLLEERIAGWKTQTSTEEVGRVVSVGDGIARLFGLEGVQAGE
LVEFQNGMTGMALNLETDNVGVVIFGDDRSVLEGDSVKRTGRIVDVPIGP
GLLGRVVDALGNPIDGKGPIPAKERRRVELKAPGIIPRKSVHEPMMTGLK
CVDALVPVGRGQRELIIGDRQTGKTAVAVDAIINQKEINDSTDDESKKLY
CIYVAVGQKRSTVAQIVKALEQRDAMKYTTVVAATASEAAPLQFLAPYSG
CAMGEWFRDSGRHCVIIYDDLSKQATAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMGDKSGGGSLTALPVIETQAGDVSAYIPTNVISITDGQI
FLETELFYKGIRPAINVGLSVSRVGSAAQVKAMKQVAGTMKLELAQYREV
AAFAQFGSDLDASTRQLLTRGTALTELLKQRQYSPMKNSVQVCVLYCGVK
GYLDPLDPKEISRFESLFIDYINANHQDILKTIETEKELSEKTEAKLRAA
VDEFVAMNEFKK
3D structure
PDB6tmh ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria.
ChainA
Resolution3.1 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) K174 Q208 K209 R373
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 A Q223 G225 K226 T227 A228 F409 R414 Q484 Q171 G173 K174 T175 A176 F357 R362 Q432
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:6tmh, PDBe:6tmh, PDBj:6tmh
PDBsum6tmh
PubMed33402698
UniProtS7UU80

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