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Mycobacterium smegmatis ATP synthase fo state 3

Analyse Mycobacterium smegmatis ATP synthase fo state 3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NL9
Type
protein
Length
1,269 residues
Chains
15
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP synthase subunit alpha; ATP synthase gamma chain; ATP synthase epsilon chain; ATP…
EC
7.1.2.2
UniProt
A0R202, A0R201, A0R1Z9, A0R205, A0R206, A0R204, A0R203
Pockets
10 · best druggability 0.83

Structure

electron microscopy · 7 distinct chains · 65% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
CATP synthase subunit alpha (EC 7.1.2.2)protein80% helix, 25% strandA0R202
GATP synthase gamma chainprotein4238% helix, 10% strandA0R201
HATP synthase epsilon chainprotein10117% helix, 41% strandA0R1Z9
L, M, N, O, P, Q, R, S, TATP synthase subunit Cprotein8488% helix, 0% strandA0R205
aATP synthase subunit aprotein23871% helix, 5% strandA0R206
bATP synthase subunit Bprotein6386% helix, 0% strandA0R204
dATP synthase subunit B-deltaprotein6197% helix, 0% strandA0R203

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15640.830.8864empty
28430.710.7677empty
31860.700.8833empty
4520.690.9719empty
51020.670.897empty

Interfaces

31 interfaces between chains.

  • L–T · 1730 Ų buried · 6 hydrogen bonds · protein-protein
  • L–M · 1686 Ų buried · 7 hydrogen bonds · protein-protein
  • a–b · 1676 Ų buried · 10 hydrogen bonds · protein-protein
  • O–P · 1673 Ų buried · 9 hydrogen bonds · protein-protein
  • P–Q · 1669 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 7NL9 · Mycobacterium smegmatis ATP synthase Fo state 3 · the same entry in another collection · chain d against d, TM-score 1.00

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