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Crystal structure of NEDD4 with a ub variant

Analyse Crystal structure of NEDD4 with a ub variant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5C7J
Type
protein
Length
916 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase NEDD4; Polyubiquitin-C
EC
6.3.2.-
UniProt
P46934, P0CG48
Pockets
10 · best druggability 0.71

Structure

x-ray diffraction · 3 distinct chains · 48% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin-protein ligase NEDD4 (EC 6.3.2.-)protein37351% helix, 13% strandP46934
BE3 ubiquitin-protein ligase NEDD4 (EC 6.3.2.-)protein37351% helix, 13% strandP46934
C, DPolyubiquitin-Cprotein8527% helix, 25% strandP0CG48

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13170.710.8446empty
22960.710.8540empty
34940.670.7845empty
44410.650.7847empty
53240.610.7850empty

Interfaces

4 interfaces between chains.

  • B–D · 763 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 756 Ų buried · 11 hydrogen bonds · protein-protein
  • A–B · 468 Ų buried · 7 hydrogen bonds · protein-protein
  • B–C · 285 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 5C7J · Crystal structure of NEDD4 with a ub variant · the same entry in another collection · chain A against A, TM-score 1.00
  • P46934 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase NEDD4 (P46934) · a predicted model of the same protein · chain B against A, TM-score 0.74

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