Research workbench
Crystal structure of S.CEREVISIAE VTA1 N-terminal domain
Analyse Crystal structure of S.CEREVISIAE VTA1 N-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RKK
- Type
- protein
- Length
- 314 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein VTA1
- UniProt
- Q06263
- Pockets
- 1 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 79% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Vacuolar protein sorting-associated protein VTA1 | protein | 157 | 79% helix, 1% strand | Q06263 |
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 | 67 | 0.46 | 0.83 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1343 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 2RKK · Crystal Structure of S.cerevisiae Vta1 N-terminal domain · 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 0.96
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 Q06263
- Elsewhere: RCSB PDB 2RKK · PDBe 2RKK · UniProt Q06263
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.