Research workbench
Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: hydration state 4A.
Analyse Low resolution structures of bovine mitochondrial F1-ATPase during controlled… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W6H
- Type
- protein
- Length
- 3,298 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase subunit alpha heart isoform, mitochondrial; ATP synthase subunit beta…
- EC
- 3.6.3.14
- UniProt
- P19483, P00829, P05631, P05630, P05632
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 8 distinct chains · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP synthase subunit alpha heart isoform, mitochondrial (EC 3.6.3.14) | protein | 487 | 43% helix, 20% strand | P19483 |
| B | ATP synthase subunit alpha heart isoform, mitochondrial (EC 3.6.3.14) | protein | 479 | 41% helix, 21% strand | P19483 |
| C | ATP synthase subunit alpha heart isoform, mitochondrial (EC 3.6.3.14) | protein | 492 | 41% helix, 20% strand | P19483 |
| D | ATP synthase subunit beta, mitochondrial (EC 3.6.3.14) | protein | 467 | 38% helix, 21% strand | P00829 |
| E, F | ATP synthase subunit beta, mitochondrial (EC 3.6.3.14) | protein | 466 | 38% helix, 21% strand | P00829 |
| G | ATP synthase subunit gamma, mitochondrial (EC 3.6.3.14) | protein | 263 | 60% helix, 12% strand | P05631 |
| H | ATP synthase subunit delta, mitochondrial (EC 3.6.3.14) | protein | 131 | 27% helix, 39% strand | P05630 |
| I | ATP synthase subunit epsilon, mitochondrial (EC 3.6.3.14) | protein | 47 | 30% helix, 6% strand | P05632 |
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 | 1010 | 0.88 | 0.90 | 100 | empty |
| 2 | 1034 | 0.87 | 0.89 | 117 | empty |
| 3 | 1077 | 0.87 | 0.89 | 118 | empty |
| 4 | 825 | 0.84 | 0.86 | 93 | empty |
| 5 | 676 | 0.83 | 0.87 | 91 | empty |
Interfaces
16 interfaces between chains.
- C–D · 2987 Ų buried · 42 hydrogen bonds · protein-protein
- A–D · 2514 Ų buried · 31 hydrogen bonds · protein-protein
- C–F · 2222 Ų buried · 21 hydrogen bonds · protein-protein
- B–F · 2150 Ų buried · 29 hydrogen bonds · protein-protein
- B–E · 1904 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2W6H · Low resolution structures of bovine mitochondrial F1-ATPase during controlled… · the same entry in another collection · chain I against I, TM-score 1.00
- P19483 · AlphaFold monomer V2.0 prediction for ATP synthase subunit alpha, mitochondrial (P19483) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P19483
- Every structure of UniProt P00829
- Every structure of UniProt P05631
- Every structure of UniProt P05630
- Every structure of UniProt P05632
- Elsewhere: RCSB PDB 2W6H · PDBe 2W6H · UniProt P19483 · UniProt P00829 · UniProt P05631 · UniProt P05630 · UniProt P05632
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