Research workbench
ATP synthase C10 ring in proton-unlocked conformation at pH 8.3
Analyse ATP synthase C10 ring in proton-unlocked conformation at pH 8.3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U2F
- Type
- protein
- Length
- 371 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP synthase subunit C, mitochondrial
- UniProt
- P61829
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| K, L, N, O | ATP synthase subunit C, mitochondrial | protein | 74 | 91% helix, 0% strand | P61829 |
| M | ATP synthase subunit C, mitochondrial | protein | 75 | 91% helix, 0% strand | P61829 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 91 | 0.32 | 0.73 | 20 | empty |
Interfaces
4 interfaces between chains.
- M–N · 1573 Ų buried · 4 hydrogen bonds · protein-protein
- K–L · 1568 Ų buried · 4 hydrogen bonds · protein-protein
- L–M · 1552 Ų buried · 4 hydrogen bonds · protein-protein
- N–O · 1540 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 modified (formylation).
Compared structures
- 3U2F · ATP synthase c10 ring in proton-unlocked conformation at PH 8.3 · the same entry in another collection · chain O against O, TM-score 1.00
- P61829 · AlphaFold monomer V2.0 prediction for ATP synthase subunit 9, mitochondrial (P61829) · a predicted model of the same protein · chain O against A, TM-score 0.97
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 P61829
- Elsewhere: RCSB PDB 3U2F · PDBe 3U2F · UniProt P61829
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