Research workbench
Crystal structure of the C subunit of V-type ATPase from thermus thermophilus
Analyse Crystal structure of the C subunit of V-type ATPase from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1V9M
- Type
- protein
- Length
- 312 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- V-type ATP synthase subunit C
- EC
- 3.6.3.14
- UniProt
- P74902
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | V-type ATP synthase subunit C (EC 3.6.3.14) | protein | 312 | 71% helix, 0% strand | P74902 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.68 | 0.81 | 38 | empty |
| 2 | 181 | 0.59 | 0.82 | 34 | empty |
| 3 | 99 | 0.42 | 0.77 | 22 | empty |
| 4 | 112 | 0.42 | 0.76 | 25 | empty |
| 5 | 89 | 0.35 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1V9M · Crystal structure of the C subunit of V-type ATPase from Thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
- P74902 · AlphaFold monomer V2.0 prediction for V-type ATP synthase subunit C (P74902) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P74902
- Elsewhere: RCSB PDB 1V9M · PDBe 1V9M · UniProt P74902
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