Research workbench
Crystal structure of the carboxy terminus of HOMER3
Analyse Crystal structure of the carboxy terminus of HOMER3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CVF
- Type
- protein
- Length
- 286 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Homer protein homolog 3
- UniProt
- Q9NSC5
- Pockets
- 2 · best druggability 0.49
Structure
x-ray diffraction · 3 distinct chains · 91% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Homer protein homolog 3 | protein | 70 | 91% helix, 0% strand | Q9NSC5 |
| C | Homer protein homolog 3 | protein | 74 | 93% helix, 0% strand | Q9NSC5 |
| D | Homer protein homolog 3 | protein | 72 | 89% helix, 0% strand | Q9NSC5 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 55 | 0.49 | 0.86 | 20 | empty |
| 2 | 128 | 0.46 | 0.78 | 19 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1085 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 1065 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 830 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 829 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 604 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
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 Q9NSC5
- Elsewhere: RCSB PDB 3CVF · PDBe 3CVF · UniProt Q9NSC5
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