MolNFT v2 · #188206 · protein
Mycobacterium smegmatis ATP synthase Fo combined class 2
7NJV: “Mycobacterium smegmatis ATP synthase Fo combined class 2”. Electron microscopy at 2.9, 1 ligand (BQ1). MolNFT v2 #188206 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7NJV
- Type
- protein
- Length
- 1,118 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.9
- Source
- Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
- UniProt
- A0R205, A0R206, A0R204, A0R203
- Ligands
- BQ1
Structure
electron microscopy · resolution 2.9 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L, M, N, O, P, Q, R, S, T | — | protein | 84 | — | A0R205 |
| a | — | protein | 238 | — | A0R206 |
| b | — | protein | 63 | — | A0R204 |
| d | — | protein | 61 | — | A0R203 |
Ligands and binding sites
- BQ1 · Bedaquiline · ligand · chains M, N, a
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7NJV · Mycobacterium smegmatis ATP synthase fo combined class 2 · the same entry in another collection · chain d against d, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0R205
- Every structure of UniProt A0R206
- Every structure of UniProt A0R204
- Every structure of UniProt A0R203
- Elsewhere: RCSB PDB 7NJV · PDBe 7NJV · UniProt A0R205 · UniProt A0R206 · UniProt A0R204 · UniProt A0R203
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