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Crystal structure of the nitrogen regulation fragment of the yeast prion protein URE2P

Analyse Crystal structure of the nitrogen regulation fragment of the yeast prion… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1HQO
Type
protein
Length
450 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
URE2 protein
UniProt
P23202
Pockets
7 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 59% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AURE2 proteinprotein22759% helix, 8% strandP23202
BURE2 proteinprotein22360% helix, 8% strandP23202

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15150.730.8236empty
26350.720.7945empty
32250.590.8029empty
41080.460.7816empty
51250.410.7522empty

Interfaces

1 interface between chains.

  • A–B · 1902 Ų buried · 24 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 1HQO · Crystal structure of the nitrogen regulation fragment of the yeast prion protein URE2P · the same entry in another collection · chain A against A, TM-score 1.00
  • P23202 · AlphaFold monomer V2.0 prediction for transcriptional regulator URE2 (P23202) · a predicted model of the same protein · chain B against A, TM-score 0.99

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