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Monobody (MC17) bound to tyrosine kinase binding domain of E3 ubiquitin ligase cbl

Analyse Monobody (MC17) bound to tyrosine kinase binding domain of E3 ubiquitin ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6O03
Type
protein
Length
774 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase cbl; Monobody (MC17)
EC
2.3.2.27
UniProt
P22681
Pockets
8 · best druggability 0.73

Structure

x-ray diffraction · 3 distinct chains · 50% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BE3 ubiquitin-protein ligase cbl (EC 2.3.2.27)protein30257% helix, 9% strandP22681
C, DMonobody (MC17)protein870% helix, 57% strand—
AE3 ubiquitin-protein ligase cbl (EC 2.3.2.27)protein29857% helix, 9% strandP22681

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111260.730.76101empty
23780.690.8243empty
32220.680.8534empty
41820.500.7726empty
51290.450.7719empty

Interfaces

5 interfaces between chains.

  • A–D · 1031 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 1012 Ų buried · 7 hydrogen bonds · protein-protein
  • B–D · 242 Ų buried · 6 hydrogen bonds · protein-protein
  • C–D · 215 Ų buried · 1 hydrogen bond · protein-protein
  • C–A · 172 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6O03 · Monobody (MC17) bound to tyrosine kinase binding domain of E3 ubiquitin ligase CBL · the same entry in another collection · chain B against B, TM-score 1.00
  • P22681 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase cbl (P22681) · a predicted model of the same protein · chain A against A, TM-score 0.97

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