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Crystal structure of REA1-MIDAS/YTM1-ubl complex from chaetomium thermophilum

Analyse Crystal structure of REA1-MIDAS/YTM1-ubl complex from chaetomium thermophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6QTB
Type
protein
Length
679 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MIDASIN,MIDASIN; Ribosome biogenesis protein YTM1
UniProt
G0SHE6, G0SFB5
Ligands
MG
Pockets
9 · best druggability 0.69

Structure

x-ray diffraction · 3 distinct chains · 45% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMIDASIN,MIDASINprotein25446% helix, 22% strandG0SHE6
B, ERibosome biogenesis protein YTM1protein8725% helix, 30% strandG0SFB5
DMIDASIN,MIDASINprotein25151% helix, 22% strandG0SHE6

Ligands and binding sites

  • MG · Magnesium ion · metal · 2 copies · chains A, B, D, E
  • GOL · Glycerol · additive · 3 copies · chains A, B, D, E

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11950.690.8728GOL
21670.670.8735empty
3940.600.8721GOL
4900.570.8622GOL
52280.530.7735empty

Interfaces

3 interfaces between chains.

  • A–D · 1314 Ų buried · 8 hydrogen bonds · protein-protein
  • D–E · 1144 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 1107 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 6QTB · Crystal structure of Rea1-MIDAS/Ytm1-UBL complex from Chaetomium thermophilum · the same entry in another collection · chain A against A, TM-score 1.00
  • G0SFB5 · AlphaFold monomer V2.0 prediction for ribosome biogenesis protein YTM1 (G0SFB5) · a predicted model of the same protein · chain B against A, TM-score 0.99

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