MolNFT v1 · #19179 · protein
EVH1 domain from ENA/VASP-like protein in complex with acta peptide
1QC6: “EVH1 domain from ENA/VASP-like protein in complex with acta peptide”. X-ray diffraction, 3 pockets (best druggability 0.42). MolNFT v1 #19179 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1QC6
- Type
- protein
- Length
- 228 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- EVH1 domain from ENA/VASP-like protein; Phe-glu-phe-pro-pro-pro-pro-thr-asp-glu-glu
- UniProt
- P70429
- Pockets
- 3 · best druggability 0.42
Structure
x-ray diffraction · 3 distinct chains · 14% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | EVH1 domain from ENA/VASP-like protein | protein | 108 | 16% helix, 52% strand | P70429 |
| C | Phe-glu-phe-pro-pro-pro-pro-thr-asp-glu-glu | protein | 7 | 0% helix, 0% strand | — |
| D | Phe-glu-phe-pro-pro-pro-pro-thr-asp-glu-glu | protein | 5 | 0% helix, 0% strand | — |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 92 | 0.42 | 0.79 | 18 | empty |
| 2 | 94 | 0.42 | 0.78 | 16 | empty |
| 3 | 54 | 0.33 | 0.78 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 740 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 344 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 336 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 1QC6 · EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P70429 · AlphaFold monomer V2.0 prediction for ENA/VASP-like protein (P70429) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 P70429
- Elsewhere: RCSB PDB 1QC6 · PDBe 1QC6 · UniProt P70429
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