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Catalysis and 5' end sensing by ribonuclease RNase J of the metallo-beta-lactamase family

Analyse Catalysis and 5' end sensing by ribonuclease RNase J of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5A0T
Type
protein + RNA
Length
915 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease J; 5'-R(*CP*GP*CP*CP*UP)-3'
UniProt
O86842
Ligands
ZN
Pockets
8 · best druggability 0.79

Structure

x-ray diffraction · 3 distinct chains · 29% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibonuclease Jprotein45429% helix, 25% strandO86842
BRibonuclease Jprotein45129% helix, 24% strandO86842
E, F5'-R(*CP*GP*CP*CP*UP)-3'rna5——

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains A, E, B, F
  • PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110170.790.8099empty
29450.720.7690empty
31180.510.8125empty
4610.460.8313empty
5670.430.8116empty

Interfaces

3 interfaces between chains.

  • A–B · 1170 Ų buried · 19 hydrogen bonds · protein-protein
  • B–F · 1020 Ų buried · 19 hydrogen bonds · protein-nucleic
  • A–E · 1011 Ų buried · 19 hydrogen bonds · protein-nucleic

Compared structures

  • 5A0T · Catalysis and 5' end sensing by ribonuclease RNase J of the metallo- beta-lactamase family · the same entry in another collection · chain A against A, TM-score 1.00

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