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Structure of ubiquitin fold protein R767E mutant

Analyse Structure of ubiquitin fold protein R767E mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2D5G
Type
protein
Length
497 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Axin-1
UniProt
O70239
Ligands
HG
Pockets
4 · best druggability 0.37

Structure

x-ray diffraction · 3 distinct chains · 6% helix, 45% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, D, FAxin-1protein836% helix, 46% strandO70239
BAxin-1protein856% helix, 45% strandO70239
EAxin-1protein806% helix, 44% strandO70239

Ligands and binding sites

  • HG · Mercury (II) ion · metal · 10 copies · chains A, B, C, D, E, F

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1900.370.7620empty
2950.370.7525empty
3760.320.7422empty
4500.240.7212empty

Interfaces

5 interfaces between chains.

  • E–F · 854 Ų buried · 13 hydrogen bonds · protein-protein
  • A–C · 838 Ų buried · 12 hydrogen bonds · protein-protein
  • A–B · 818 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 815 Ų buried · 12 hydrogen bonds · protein-protein
  • D–E · 697 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 2D5G · Structure of ubiquitin fold protein R767E mutant · the same entry in another collection · chain F against F, TM-score 1.00
  • O70239 · AlphaFold monomer V2.0 prediction for axin-1 (O70239) · a predicted model of the same protein · chain C against A, TM-score 0.97

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