Research workbench
Mycobacterium smegmatis ATP synthase fo combined class 2
Analyse Mycobacterium smegmatis ATP synthase fo combined class 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NJV
- Type
- protein
- Length
- 1,118 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0R205, A0R206, A0R204, A0R203
- Ligands
- BQ1
Structure
electron microscopy · 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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