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Crystal structure of the phosphorolytic exoribonuclease RNase pH from bacillus subtilis

Analyse Crystal structure of the phosphorolytic exoribonuclease RNase pH from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1OYR
Type
protein
Length
1,452 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease pH
EC
2.7.7.56
UniProt
P28619
Ligands
CD, SO4
Pockets
8 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FRibonuclease pH (EC 2.7.7.56)protein24233% helix, 30% strandP28619

Ligands and binding sites

  • CD · Cadmium ion · metal · 3 copies · chains A, E, D
  • SO4 · Sulfate ion · ion · 12 copies · chains A, B, C, D, E, F

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

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17670.770.8198SO4
210420.750.78131SO4
36400.740.8183SO4
41430.670.8832empty
51560.640.8632empty

Interfaces

12 interfaces between chains.

  • D–E · 1560 Ų buried · 26 hydrogen bonds · protein-protein
  • A–F · 1466 Ų buried · 23 hydrogen bonds · protein-protein
  • B–C · 1401 Ų buried · 33 hydrogen bonds · protein-protein
  • C–D · 1398 Ų buried · 19 hydrogen bonds · protein-protein
  • E–F · 1346 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 1OYR · Crystal structure of the phosphorolytic exoribonuclease RNase PH from Bacillus subtilis · the same entry in another collection · chain C against C, TM-score 1.00
  • P28619 · AlphaFold monomer V2.0 prediction for ribonuclease pH (P28619) · a predicted model of the same protein · chain A against A, TM-score 0.99

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