Research workbench
MEF2B Apo Protein Structure
Analyse MEF2B Apo Protein Structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C9L
- Type
- protein
- Length
- 479 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- Homo sapiens
- Molecule
- Myocyte-specific enhancer factor 2B
- UniProt
- Q02080
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · resolution 2.3 · 5 distinct chains · 56% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Myocyte-specific enhancer factor 2B | protein | 84 | 54% helix, 19% strand | Q02080 |
| B | Myocyte-specific enhancer factor 2B | protein | 85 | 56% helix, 19% strand | Q02080 |
| C | Myocyte-specific enhancer factor 2B | protein | 85 | 55% helix, 19% strand | Q02080 |
| E | Myocyte-specific enhancer factor 2B | protein | 64 | 56% helix, 19% strand | Q02080 |
| F | Myocyte-specific enhancer factor 2B | protein | 77 | 58% helix, 16% strand | Q02080 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 714 | 0.67 | 0.75 | 57 | empty |
| 2 | 108 | 0.44 | 0.78 | 21 | empty |
| 3 | 70 | 0.36 | 0.77 | 17 | empty |
| 4 | 101 | 0.31 | 0.72 | 23 | empty |
Interfaces
6 interfaces between chains.
- C–D · 3013 Ų buried · 42 hydrogen bonds · protein-protein
- A–B · 2962 Ų buried · 39 hydrogen bonds · protein-protein
- E–F · 2012 Ų buried · 25 hydrogen bonds · protein-protein
- D–F · 406 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 129 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 Q02080
- Elsewhere: RCSB PDB 6C9L · PDBe 6C9L · UniProt Q02080
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