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Mycobacterium smegmatis ATP synthase F1 state 2

Analyse Mycobacterium smegmatis ATP synthase F1 state 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NKH
Type
protein
Length
2,959 residues
Chains
7
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
A0R202, A0R200, A0R201
Ligands
ATP, ADP, MG

Structure

electron microscopy · 7 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein493—A0R202
B—protein486—A0R202
C—protein492—A0R202
D—protein467—A0R200
E—protein464—A0R200
F—protein468—A0R200
G—protein89—A0R201

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains A, D, B, E, C, F
  • ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains C, D, E
  • MG · Magnesium ion · metal · 5 copies · chains A, B, C, D, F

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 7NKH · Mycobacterium smegmatis ATP synthase F1 state 2 · the same entry in another collection · chain G against G, TM-score 1.00
  • A0R202 · AlphaFold monomer V2.0 prediction for ATP synthase subunit alpha (A0R202) · a predicted model of the same protein · chain C against A, TM-score 0.99
  • A0R200 · AlphaFold monomer V2.0 prediction for ATP synthase subunit beta (A0R200) · a predicted model of the same protein · chain E against A, TM-score 0.97
  • A0R201 · AlphaFold monomer V2.0 prediction for ATP synthase gamma chain (A0R201) · a predicted model of the same protein · chain G against A, TM-score 0.97

Analyse

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