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Cryo-EM structure of tetrahymena thermophila mitochondrial ATP synthase - central STALK/CRING

Analyse Cryo-EM structure of tetrahymena thermophila mitochondrial ATP synthase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6YNW
Type
protein
Length
1,176 residues
Chains
13
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Subunit C; Subunit gamma; Subunit delta; Subunit epsilon
EC
3.6.1.34
UniProt
Q951A5, Q22Z05, Q22ZH1, I7MMW3
Pockets
8 · best druggability 0.79

Structure

electron microscopy · 4 distinct chains · 47% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
P, O, N, M, L, K, J, I, H, QSubunit C (EC 3.6.1.34)protein7595% helix, 0% strandQ951A5
gSubunit gammaprotein22454% helix, 15% strandQ22Z05
dSubunit deltaprotein13418% helix, 40% strandQ22ZH1
eSubunit epsilonprotein6831% helix, 15% strandI7MMW3

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19690.790.81105empty
25330.770.8457empty
36810.640.7473empty
42260.600.8127empty
52680.560.7529empty

Interfaces

32 interfaces between chains.

  • H–Q · 1613 Ų buried · 1 hydrogen bond · protein-protein
  • J–I · 1603 Ų buried · 3 hydrogen bonds · protein-protein
  • N–M · 1601 Ų buried · 1 hydrogen bond · protein-protein
  • I–H · 1600 Ų buried · 4 hydrogen bonds · protein-protein
  • L–K · 1573 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 6YNW · Cryo-EM structure of Tetrahymena thermophila mitochondrial ATP synthase - central… · the same entry in another collection · chain P against P, TM-score 1.00

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