MolNFT v1 · #158637 · protein

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

6O02 · E3 ubiquitin-protein ligase cbl: “Monobody (MC3) bound to tyrosine kinase binding domain of E3 ubiquitin ligase cbl”. X-ray diffraction, 2 pockets (best druggability 0.77). MolNFT v1 #158637 on GenesisL1: 3D structure, binding sites…

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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