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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).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DMyocyte-specific enhancer factor 2Bprotein8454% helix, 19% strandQ02080
BMyocyte-specific enhancer factor 2Bprotein8556% helix, 19% strandQ02080
CMyocyte-specific enhancer factor 2Bprotein8555% helix, 19% strandQ02080
EMyocyte-specific enhancer factor 2Bprotein6456% helix, 19% strandQ02080
FMyocyte-specific enhancer factor 2Bprotein7758% helix, 16% strandQ02080

Pockets

4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17140.670.7557empty
21080.440.7821empty
3700.360.7717empty
41010.310.7223empty

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

  • 6C9L · MEF2B apo protein structure · the same entry in another collection · chain F against F, TM-score 1.00
  • Q02080 · AlphaFold monomer V2.0 prediction for myocyte-specific enhancer factor 2B (Q02080) · a predicted model of the same protein · chain E against A, TM-score 0.96

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