GL1X · GenesisL1 explorer

Research workbench

Alternative conformations of NOP56/58-fibrillarin complex and implication for induced-fit assenly of box C/D rnps

Analyse Alternative conformations of NOP56/58-fibrillarin complex and implication for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NNW
Type
protein
Length
1,154 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NOP5/NOP56 related protein; Fibrillarin-like RRNA/TRNA 2'-O-methyltransferase
EC
2.1.1.-
UniProt
Q8U4M1, Q8U4M2
Pockets
10 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CNOP5/NOP56 related proteinprotein35066% helix, 5% strandQ8U4M1
B, DFibrillarin-like RRNA/TRNA 2'-O-methyltransferase (EC 2.1.1.-)protein22729% helix, 30% strandQ8U4M2

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13540.640.7949empty
23380.640.7946empty
32280.570.7921empty
43030.560.7629empty
51980.540.7922empty

Interfaces

3 interfaces between chains.

  • C–D · 1951 Ų buried · 22 hydrogen bonds · protein-protein
  • A–B · 1946 Ų buried · 19 hydrogen bonds · protein-protein
  • A–C · 332 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 2NNW · Alternative conformations of Nop56/58-fibrillarin complex and implication for induced-fit… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8U4M2 · AlphaFold monomer V2.0 prediction for fibrillarin-like RRNA/TRNA 2'-O-methyltransferase… · a predicted model of the same protein · chain D against A, TM-score 0.99

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.