Structure of PDB 6ynz Chain A2

Receptor sequence
>6ynzA2 (length=512) Species: 5911 (Tetrahymena thermophila) [Search protein sequence]
LSTGEASVVLAEKIKGITQQNDITEYGTVISIGDGIARVFGLTKVQAGEM
VEFKSGIRGMALNLETDNVGVVVLGNDRDIKEGDVVKRTGAIVDVPIGEA
MCGRVFDALGNPIDGLGPLKTTQRARVEIKAPGIIPRQSVRQPMQTGIKC
VDSLVPIGRGQRELIIGDRQTGKTAIAIDTILNQKEAFNTGDVKKQLYCI
YVAVGQKRSTIANLVSILKQHDCMKFTIVVCATASDAAPLQFLAPYSGCA
IGEFFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLH
SRLLERAAKMNDSLGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFL
ETELFYKGIRPAINVGLSVSRVGSAAQIKAMKKIAGNLKLTLATYRELAA
FSQFGSDLDAKTQQQLNTGERLVEMLKQNQYTPMKVEEQVCIIFAGVKGF
LDALVTSEVLKFEKKFLEHVRTNHSALLKRIRDSGDLSEVDTNELNTIIP
LFIQEGGFKLKA
3D structure
PDB6ynz Type III ATP synthase is a symmetry-deviated dimer that induces membrane curvature through tetramerization.
ChainA2
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) K173 Q206 K207 R371
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 ADP A2 S403 R404 S370 R371
BS02 ATP A2 Q203 T204 G205 K206 T207 A208 F388 Q463 Q170 T171 G172 K173 T174 A175 F355 Q430
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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