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Crystal structure of yeast RNase III (RNT1P) complexed with the product of dsrna processing

Analyse Crystal structure of yeast RNase III (RNT1P) complexed with the product of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4OOG
Type
protein + RNA
Length
514 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease 3; 34-mer RNA
EC
3.1.26.3
UniProt
Q02555
Ligands
MG
Pockets
4 · best druggability 0.61

Structure

x-ray diffraction · 4 distinct chains · 63% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibonuclease 3protein10970% helix, 0% strandQ02555
BRibonuclease 3protein11068% helix, 0% strandQ02555
CRibonuclease 3 (EC 3.1.26.3)protein26157% helix, 8% strandQ02555
D34-mer RNArna34——

Ligands and binding sites

  • MG · Magnesium ion · metal · 4 copies · chains C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12710.610.8024empty
25090.580.7427MG
33390.570.7634empty
41110.400.7619empty

Interfaces

6 interfaces between chains.

  • A–B · 3578 Ų buried · 23 hydrogen bonds · protein-protein
  • C–D · 1552 Ų buried · 39 hydrogen bonds · protein-nucleic
  • A–C · 300 Ų buried · 2 hydrogen bonds · protein-protein
  • A–D · 163 Ų buried · 1 hydrogen bond · protein-nucleic
  • B–C · 121 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4OOG · Crystal structure of yeast RNase III (Rnt1p) complexed with the product of dsRNA… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q02555 · AlphaFold monomer V2.0 prediction for ribonuclease 3 (Q02555) · a predicted model of the same protein · chain C against A, TM-score 1.00

Analyse

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