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Structure of NEDD4L WW3 domain

Analyse Structure of NEDD4L WW3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7LP2
Type
protein
Length
141 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase; Angiomotin
EC
2.3.2.26
UniProt
A0A6Q8PG51, Q4VCS5
Ligands
SO4
Pockets
1 · best druggability 0.65

Structure

x-ray diffraction · 5 distinct chains · 8% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CE3 ubiquitin-protein ligase (EC 2.3.2.26)protein330% helix, 42% strandA0A6Q8PG51
BAngiomotinprotein1127% helix, 0% strandQ4VCS5
DAngiomotinprotein1225% helix, 0% strandQ4VCS5
EE3 ubiquitin-protein ligase (EC 2.3.2.26)protein370% helix, 35% strandA0A6Q8PG51
FAngiomotinprotein1520% helix, 0% strandQ4VCS5

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains E, F, D
  • GOL · Glycerol · additive · 2 copies · chains C, E

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11030.650.8936empty

Interfaces

11 interfaces between chains.

  • E–F · 552 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 529 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 489 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 382 Ų buried · 4 hydrogen bonds · protein-protein
  • A–F · 327 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 7LP2 · Structure of Nedd4L WW3 domain · the same entry in another collection · chain C against C, TM-score 1.00
  • Q4VCS5 · AlphaFold monomer V2.0 prediction for angiomotin (Q4VCS5) · a predicted model of the same protein · chain B against A, TM-score 0.35

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