MolNFT v1 · #158895 · protein
Saccharomyces cerevisiae V-ATPase VPH1-vo
6O7T · V-type proton ATPase subunit a, vacuolar isoform: “Saccharomyces cerevisiae V-ATPase VPH1-vo”. Electron microscopy, 20 pockets (best druggability 0.80). MolNFT v1 #158895 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6O7T
- Type
- protein
- Length
- 2,824 residues
- Chains
- 15
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- V-type proton ATPase subunit a, vacuolar isoform; V0 assembly protein 1; V-type proton…
- UniProt
- P32563, P53262, P23968, P32366, P0C5R9, P25515, P32842, Q3E7B6
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 11 distinct chains · 64% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| a | V-type proton ATPase subunit a, vacuolar isoform | protein | 734 | 54% helix, 7% strand | P32563 |
| b | V0 assembly protein 1 | protein | 38 | 76% helix, 0% strand | P53262 |
| c | V-type proton ATPase subunit C'' | protein | 195 | 69% helix, 0% strand | P23968 |
| d | V-type proton ATPase subunit D | protein | 314 | 54% helix, 0% strand | P32366 |
| f | Putative protein YPR170W-B | protein | 63 | 68% helix, 0% strand | P0C5R9 |
| g | V-type proton ATPase subunit C | protein | 155 | 77% helix, 0% strand | P25515 |
| h | V-type proton ATPase subunit C | protein | 159 | 74% helix, 0% strand | P25515 |
| i, j, k, m, n | V-type proton ATPase subunit C | protein | 158 | 70% helix, 0% strand | P25515 |
| l | V-type proton ATPase subunit C | protein | 156 | 77% helix, 0% strand | P25515 |
| o | V-type proton ATPase subunit C' | protein | 156 | 69% helix, 0% strand | P32842 |
| e | V-type proton ATPase subunit E | protein | 64 | 67% helix, 3% strand | Q3E7B6 |
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 | 1149 | 0.80 | 0.81 | 92 | empty |
| 2 | 991 | 0.80 | 0.82 | 67 | empty |
| 3 | 883 | 0.75 | 0.78 | 70 | empty |
| 4 | 594 | 0.70 | 0.79 | 55 | empty |
| 5 | 90 | 0.70 | 0.94 | 26 | empty |
Interfaces
31 interfaces between chains.
- a–e · 2074 Ų buried · 17 hydrogen bonds · protein-protein
- c–g · 1727 Ų buried · 4 hydrogen bonds · protein-protein
- h–i · 1688 Ų buried · 5 hydrogen bonds · protein-protein
- n–o · 1669 Ų buried · 5 hydrogen bonds · protein-protein
- c–o · 1663 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6O7T · Saccharomyces cerevisiae V-ATPase Vph1-VO · the same entry in another collection · chain l against l, 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
- Every structure of UniProt P32563
- Every structure of UniProt P53262
- Every structure of UniProt P23968
- Every structure of UniProt P32366
- Every structure of UniProt P0C5R9
- Every structure of UniProt P25515
- Every structure of UniProt P32842
- Every structure of UniProt Q3E7B6
- Elsewhere: RCSB PDB 6O7T · PDBe 6O7T · UniProt P32563 · UniProt P53262 · UniProt P23968 · UniProt P32366 · UniProt P0C5R9 · UniProt P25515 · UniProt P32842 · UniProt Q3E7B6
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