Research workbench
Autoinhibited VAV1
Analyse Autoinhibited VAV1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KY9
- Type
- protein
- Length
- 1,071 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proto-oncogene vav
- UniProt
- P15498
- Ligands
- ZN
- Pockets
- 16 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proto-oncogene vav | protein | 530 | 54% helix, 12% strand | P15498 |
| B | Proto-oncogene vav | protein | 541 | 54% helix, 12% strand | P15498 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 588 | 0.71 | 0.79 | 67 | empty |
| 2 | 424 | 0.70 | 0.81 | 43 | empty |
| 3 | 509 | 0.69 | 0.80 | 53 | empty |
| 4 | 340 | 0.67 | 0.81 | 35 | empty |
| 5 | 52 | 0.66 | 0.95 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 473 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P15498
- Elsewhere: RCSB PDB 3KY9 · PDBe 3KY9 · UniProt P15498
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