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The conformation of the epsilon and gamma subunits within the E. COLI F1 ATPase
Analyse The conformation of the epsilon and gamma subunits within the E. COLI F1 ATPase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JNV
- Type
- protein
- Length
- 3,268 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase alpha chain; ATP synthase beta chain; ATP synthase epsilon chain; ATP…
- EC
- 3.6.1.34
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 6 distinct chains · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATP synthase alpha chain (EC 3.6.1.34) | protein | 487 | 43% helix, 21% strand | — |
| C | ATP synthase alpha chain (EC 3.6.1.34) | protein | 492 | 41% helix, 20% strand | — |
| D | ATP synthase beta chain (EC 3.6.1.34) | protein | 467 | 38% helix, 21% strand | — |
| E, F | ATP synthase beta chain (EC 3.6.1.34) | protein | 466 | 38% helix, 21% strand | — |
| Y | ATP synthase epsilon chain (EC 3.6.1.34) | protein | 130 | 28% helix, 43% strand | — |
| Z | ATP synthase gamma chain (EC 3.6.1.34) | protein | 273 | 62% helix, 16% strand | — |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1061 | 0.81 | 0.83 | 138 | empty |
| 2 | 1172 | 0.79 | 0.82 | 138 | empty |
| 3 | 1189 | 0.79 | 0.82 | 140 | empty |
| 4 | 782 | 0.75 | 0.81 | 113 | empty |
| 5 | 670 | 0.74 | 0.81 | 109 | empty |
Interfaces
13 interfaces between chains.
- C–D · 529 Ų buried · 5 hydrogen bonds · protein-protein
- Y–Z · 464 Ų buried · 6 hydrogen bonds · protein-protein
- B–F · 435 Ų buried · 5 hydrogen bonds · protein-protein
- A–E · 389 Ų buried · 5 hydrogen bonds · protein-protein
- C–F · 349 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1JNV · The Conformation of the Epsilon and Gamma Subunits within the E. coli F1 ATPase · 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
- Elsewhere: RCSB PDB 1JNV · PDBe 1JNV
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