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Crystal structure of apo C-cbl tkbd refined to 2.25 a resolution

Analyse Crystal structure of apo C-cbl tkbd refined to 2.25 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5HKW
Type
protein
Length
906 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase cbl
EC
6.3.2.-
UniProt
P22681
Ligands
NA
Pockets
14 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 9% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CE3 ubiquitin-protein ligase cbl (EC 6.3.2.-)protein30259% helix, 9% strandP22681

Ligands and binding sites

  • NA · Sodium ion · metal · 3 copies · chains A, B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19120.710.76109empty
25280.650.7650empty
33550.550.7441empty
41610.510.7921empty
51210.490.8023empty

Interfaces

2 interfaces between chains.

  • A–C · 755 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 752 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 5HKW · Crystal Structure of Apo c-Cbl TKBD Refined to 2.25 A Resolution · 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 C against A, TM-score 0.96

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