MolNFT v1 · #11475 · protein
The conformation of the epsilon and gamma subunits within the E. COLI F1 ATPase
1JNV · ATP synthase alpha chain: “The conformation of the epsilon and gamma subunits within the E. COLI F1 ATPase”. X-ray diffraction, 20 pockets (best druggability 0.81). MolNFT v1 #11475 on GenesisL1: 3D structure, binding sites and…
- 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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