MolNFT v1 · #178609 · protein
Cryo-EM structure of bedaquiline-saturated mycobacterium smegmatis ATP synthase fo region
7JGC: “Cryo-EM structure of bedaquiline-saturated mycobacterium smegmatis ATP synthase fo region”. Electron microscopy, 1 ligand (BQ1). MolNFT v1 #178609 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7JGC
- Type
- protein
- Length
- 1,017 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0R206, A0A0D6IV98, A0R203, Q5TIX5
- Ligands
- BQ1
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| a | — | protein | 207 | — | A0R206 |
| b | — | protein | 41 | — | A0A0D6IV98 |
| d | — | protein | 40 | — | A0R203 |
| 1, 2, 3, 4, 5, 6, 7, 8, 9 | — | protein | 81 | — | Q5TIX5 |
Ligands and binding sites
- BQ1 · Bedaquiline · ligand · 7 copies · chains a, 1, 2, 4, 5, 6, 7, 8, 9
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7JGC · Cryo-EM structure of bedaquiline-saturated Mycobacterium smegmatis ATP synthase FO region · the same entry in another collection · chain 9 against 9, 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 A0R206
- Every structure of UniProt A0A0D6IV98
- Every structure of UniProt A0R203
- Every structure of UniProt Q5TIX5
- Elsewhere: RCSB PDB 7JGC · PDBe 7JGC · UniProt A0R206 · UniProt A0A0D6IV98 · UniProt A0R203 · UniProt Q5TIX5
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