Structure of PDB 6tmk Chain D2

Receptor sequence
>6tmkD2 (length=475) Species: 507601 (Toxoplasma gondii GT1) [Search protein sequence]
NHGRITQVIGAVVDVHFDEQLPPILNSLEVQGHTNRLVLEVAQHLGENTV
RTIAMDATEGLVRGQKVVDTGAPIQVPVGVETLGRIMNVIGEPVDECGPV
PAKKTYSIHRAAPLFADQSTEPGLLQTGIKVVDLLAPYAKGGKIGLFGGA
GVGKTVLIMELINNVANKHGGFSVFAGVGERTREGNDLYHEMMTTGVIKR
KKLEDGKFDFTGSKAALVYGQMNEPPGARARVALTALSVAEYFRDEQGQD
VLLFIDNIYRFTQAGSEVSALLGRIPSAVGYQPTLATDLGQLQERITTTK
KGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRQIAELGIYPAVDP
LDSTSRMLAPEIVGQEHYDTARATQKLLQDYKSLQDIIAILGMDELSEED
KLVVSRARKIQRFLSQPFTVAEVFTGKPGRFVELPETIKSAQTILRGECD
DLPEMAFYMCGGLEEVRSKAVKMAQ
3D structure
PDB6tmk ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria.
ChainD2
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) K233 E259 R260 R435
Catalytic site (residue number reindexed from 1) K154 E180 R181 R356
Enzyme Commision number 7.1.2.2: H(+)-transporting two-sector ATPase.
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 ADP D2 G230 G232 K233 T234 V235 Y424 F503 G151 G153 K154 T155 V156 Y345 F424
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
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:0015986 proton motive force-driven ATP synthesis
GO:0042776 proton motive force-driven mitochondrial ATP synthesis
GO:0046034 ATP metabolic process
GO:1902600 proton transmembrane transport
Cellular Component
GO:0005739 mitochondrion
GO:0009507 chloroplast
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
UniProtA0A125YYY4

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