Research workbench
Mycobacterium smegmatis ATP synthase fo combined class 4
Analyse Mycobacterium smegmatis ATP synthase fo combined class 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NJX
- Type
- protein
- Length
- 1,118 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase subunit C; ATP synthase subunit a; ATP synthase subunit B; ATP synthase…
- UniProt
- A0R205, A0R206, A0R204, A0R203
- Pockets
- 11 · best druggability 0.84
Structure
electron microscopy · 4 distinct chains · 80% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L, M, N, O, P, Q, R, S, T | ATP synthase subunit C | protein | 84 | 85% helix, 0% strand | A0R205 |
| a | ATP synthase subunit a | protein | 238 | 73% helix, 5% strand | A0R206 |
| b | ATP synthase subunit B | protein | 63 | 84% helix, 0% strand | A0R204 |
| d | ATP synthase subunit B-delta | protein | 61 | 95% helix, 0% strand | A0R203 |
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 792 | 0.84 | 0.86 | 62 | empty |
| 2 | 324 | 0.76 | 0.87 | 50 | empty |
| 3 | 181 | 0.75 | 0.91 | 39 | empty |
| 4 | 120 | 0.62 | 0.85 | 8 | empty |
| 5 | 400 | 0.62 | 0.76 | 56 | empty |
Interfaces
18 interfaces between chains.
- a–b · 1733 Ų buried · 11 hydrogen bonds · protein-protein
- Q–R · 1690 Ų buried · 5 hydrogen bonds · protein-protein
- O–P · 1668 Ų buried · 9 hydrogen bonds · protein-protein
- P–Q · 1654 Ų buried · 5 hydrogen bonds · protein-protein
- L–T · 1627 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 7NJX · Mycobacterium smegmatis ATP synthase Fo combined class 4 · 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 7NJX · PDBe 7NJX · UniProt A0R205 · UniProt A0R206 · UniProt A0R204 · UniProt A0R203
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