Research workbench
EVH1 domain from murine homer 2B/VESL 2
Analyse EVH1 domain from murine homer 2B/VESL 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1I7A
- Type
- protein
- Length
- 415 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homer 2B; Phe-ala-phe
- UniProt
- Q9QWW1
- Ligands
- PHE
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Homer 2B | protein | 103 | 17% helix, 49% strand | Q9QWW1 |
| E | Phe-ala-phe | protein | 3 | 0% helix, 0% strand | — |
Ligands and binding sites
- PHE · Phenylalanine · ligand · 3 copies · chains A, B, C, D
- FLC · Citrate anion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 293 | 0.70 | 0.84 | 32 | PHE |
| 2 | 87 | 0.32 | 0.74 | 14 | empty |
| 3 | 82 | 0.30 | 0.72 | 18 | empty |
Interfaces
6 interfaces between chains.
- C–D · 429 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 428 Ų buried · 2 hydrogen bonds · protein-protein
- A–E · 266 Ų buried · 1 hydrogen bond · protein-protein
- B–E · 264 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 45 Ų buried · 2 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 Q9QWW1
- Elsewhere: RCSB PDB 1I7A · PDBe 1I7A · UniProt Q9QWW1
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