Research workbench
NMR structure of the VTA1NTD-DID2(176-204) complex
Analyse NMR structure of the VTA1NTD-DID2(176-204) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5H7P
- Type
- protein
- Length
- 196 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein VTA1; Vacuolar protein-sorting-associated…
- UniProt
- Q06263, P69771
- Pockets
- 5 · best druggability 0.57
Structure
solution nmr · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vacuolar protein sorting-associated protein VTA1 | protein | 167 | 84% helix, 0% strand | Q06263 |
| B | Vacuolar protein-sorting-associated protein 46 | protein | 29 | 62% helix, 0% strand | P69771 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.57 | 0.79 | 33 | empty |
| 2 | 178 | 0.56 | 0.80 | 29 | empty |
| 3 | 165 | 0.55 | 0.80 | 27 | empty |
| 4 | 123 | 0.48 | 0.79 | 23 | empty |
| 5 | 103 | 0.45 | 0.78 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 482 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 5H7P · NMR structure of the Vta1NTD-Did2(176-204) complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q06263 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein VTA1… · a predicted model of the same protein · chain A against A, TM-score 0.79
- P69771 · AlphaFold monomer V2.0 prediction for vacuolar protein-sorting- associated protein 46… · a predicted model of the same protein · chain B against A, TM-score 0.60
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 Q06263
- Every structure of UniProt P69771
- Elsewhere: RCSB PDB 5H7P · PDBe 5H7P · UniProt Q06263 · UniProt P69771
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