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Crystal structure of the thioredoxin-fold domain of human phosducin- like protein 2

Analyse Crystal structure of the thioredoxin-fold domain of human phosducin- like… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EVI
Type
protein
Length
236 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Phosducin-like protein 2
UniProt
Q8N4E4
Ligands
NA
Pockets
1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BPhosducin-like protein 2protein11834% helix, 24% strandQ8N4E4

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A, B
  • PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B

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
13400.620.7832PEG

Interfaces

1 interface between chains.

  • A–B · 420 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 3EVI · Crystal structure of the thioredoxin-fold domain of human phosducin-like protein 2 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8N4E4 · AlphaFold monomer V2.0 prediction for phosducin-like protein 2 (Q8N4E4) · a predicted model of the same protein · chain A against A, TM-score 0.98

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