Structure of PDB 6yny Chain E2

Receptor sequence
>6ynyE2 (length=470) Species: 5911 (Tetrahymena thermophila) [Search protein sequence]
KANGQVSQVIGAVVDVQFEGELPQILNALEVQGTQHRLVLEVAQHLGDSR
VRTIAMDSTEGLVRGQPVVDTGLPISVPVGPGTLGRIMNVIGEPIDQRGP
IKAAKLYPIHRDAPSFTDQATSAEILVTGIKVVDLLAPYARGGKIGLFGG
AGVGKTVLIQELINNVAKHHGGYSVFAGVGERTREGNDLYHEMMDSKVIS
VKEGESRCALIFGQMNEPPGARARVGLTGLTVAEYFRDEEGKDVLLFVDN
IFRFTQACSEVSALLGRIPSAVGYQPTLATDLGALQERITTTQKGSITSV
QAIYVPADDLTDPAPATTFAHLDATTVLNRGLTELGIYPAVDPLDSTSRM
LDPITIGEEHYTVARGVQKLLQDYKSLQDIIAILGVDDLSEEDKLVVARA
RKVQKFLSQPFFMSEVFSGIPGRFVNLKQNIASFKALLEGAGDEYPESCF
YMKGDLEESLAAGRADALKS
3D structure
PDB6yny Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.
ChainE2
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K181 E207 R208 R375
Catalytic site (residue number reindexed from 1) K155 E181 R182 R349
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 E2 G178 G180 K181 T182 V183 Y364 F437 S440 F443 G152 G154 K155 T156 V157 Y338 F411 S414 F417
Gene Ontology
Molecular Function
GO:0005524 ATP binding
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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Cellular Component
External links
PDB RCSB:6yny, PDBe:6yny, PDBj:6yny
PDBsum6yny
PubMed33093501
UniProtI7LZV1

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