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Structure of the cs domain of the essential H/ACA rnp assembly protein SHQ1P

Analyse Structure of the cs domain of the essential H/ACA rnp assembly protein SHQ1P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EUD
Type
protein
Length
577 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein SHQ1
UniProt
P40486
Pockets
9 · best druggability 0.48

Structure

x-ray diffraction · 3 distinct chains · 3% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein SHQ1protein994% helix, 46% strandP40486
B, C, EProtein SHQ1protein984% helix, 46% strandP40486
D, FProtein SHQ1protein920% helix, 49% strandP40486

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11220.480.7918empty
21350.440.7634empty
31020.440.7922empty
41030.430.7816empty
5770.400.7923empty

Interfaces

7 interfaces between chains.

  • D–F · 854 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 655 Ų buried · 8 hydrogen bonds · protein-protein
  • B–F · 563 Ų buried · 8 hydrogen bonds · protein-protein
  • A–D · 557 Ų buried · 11 hydrogen bonds · protein-protein
  • E–F · 532 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 3EUD · Structure of the CS domain of the essential H/ACA RNP assembly protein Shq1p · the same entry in another collection · chain F against F, TM-score 1.00
  • P40486 · AlphaFold monomer V2.0 prediction for protein SHQ1 (P40486) · a predicted model of the same protein · chain A against A, TM-score 0.95

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