Structure of PDB 6ynz Chain C5

Receptor sequence
>6ynzC5 (length=513) Species: 5911 (Tetrahymena thermophila) [Search protein sequence]
KKLSTGEASVVLAEKIKGITQQNDITEYGTVISIGDGIARVFGLTKVQAG
EMVEFKSGIRGMALNLETDNVGVVVLGNDRDIKEGDVVKRTGAIVDVPIG
EAMCGRVFDALGNPIDGLGPLKTTQRARVEIKAPGIIPRQSVRQPMQTGI
KCVDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKEAFNTGDVKKQLY
CIYVAVGQKRSTIANLVSILKQHDCMKFTIVVCATASDAAPLQFLAPYSG
CAIGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFY
LHSRLLERAAKMNDSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQI
FLETELFYKGIRPAINVGLSVSRVGSAAQIKAMKKIAGNLKLTLATYREL
AAFSQFGSDLDAKTQQQLNTGERLVEMLKQNQYTPMKVEEQVCIIFAGVK
GFLDALVTSEVLKFEKKFLEHVRTNHSALLKRIRDSGDLSEVDTNELNTI
IPLFIQEGGFKLK
3D structure
PDB6ynz Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.
ChainC5
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) K206 Q239 K240 R404
Catalytic site (residue number reindexed from 1) K175 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 C5 Q203 G205 K206 T207 A208 F388 Q463 Q172 G174 K175 T176 A177 F357 Q432
Gene Ontology
Molecular Function
GO:0005524 ATP binding
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:6ynz, PDBe:6ynz, PDBj:6ynz
PDBsum6ynz
PubMed33093501
UniProtQ24HY8

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