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Monobody (MC3) bound to tyrosine kinase binding domain of E3 ubiquitin ligase cbl

Analyse Monobody (MC3) 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: 6O02
Type: protein
Length: 400 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: E3 ubiquitin-protein ligase cbl; Monobody (MC3)
EC: 2.3.2.27
UniProt: P22681
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	E3 ubiquitin-protein ligase cbl (EC 2.3.2.27)	protein	306	57% helix, 9% strand	P22681
B	Monobody (MC3)	protein	94	3% helix, 53% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1026	0.77	0.79	98	empty
2	51	0.31	0.77	14	empty

Interfaces

1 interface between chains.

A–B · 600 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6O02 · Monobody (MC3) bound to tyrosine kinase binding domain of E3 ubiquitin ligase CBL · the same entry in another collection · chain A against A, 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

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 P22681
Elsewhere: RCSB PDB 6O02 · PDBe 6O02 · UniProt P22681

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