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Crystal structure of the tyrosine kinase binding domain of cbl-C

Analyse Crystal structure of the tyrosine kinase binding domain of cbl-C in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VRN
Type: protein
Length: 290 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Signal transduction protein cbl-C
UniProt: Q9ULV8
Ligands: CA
Pockets: 4 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 54% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Signal transduction protein cbl-C	protein	290	54% helix, 9% strand	Q9ULV8

Ligands and binding sites

CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

4 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	73	0.61	0.89	26	empty
2	117	0.39	0.75	17	empty
3	54	0.30	0.76	14	empty
4	66	0.29	0.73	18	empty

Compared structures

3VRN · Crystal structure of the tyrosine kinase binding domain of Cbl-c · the same entry in another collection · chain A against A, TM-score 1.00
Q9ULV8 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase cbl-C (Q9ULV8) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9ULV8
Elsewhere: RCSB PDB 3VRN · PDBe 3VRN · UniProt Q9ULV8

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