Research workbench
VTI1B habc domain - epsinr enth domain complex
Analyse VTI1B habc domain - epsinr enth domain complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V8S
- Type
- protein
- Length
- 230 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Clathrin interactor 1; Vesicle transport through interaction with T-snares homolog 1B
- UniProt
- Q14677, Q96J28
- Pockets
- 1 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Clathrin interactor 1 | protein | 137 | 71% helix, 2% strand | Q14677 |
| V | Vesicle transport through interaction with T-snares homolog 1B | protein | 93 | 74% helix, 1% strand | Q96J28 |
Ligands and binding sites
- GOL · Glycerol · additive · 5 copies · chains E, V
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.64 | 0.81 | 39 | GOL |
Interfaces
1 interface between chains.
- E–V · 736 Ų buried · 13 hydrogen bonds · protein-protein
Compared structures
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 Q14677
- Every structure of UniProt Q96J28
- Elsewhere: RCSB PDB 2V8S · PDBe 2V8S · UniProt Q14677 · UniProt Q96J28
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.