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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
1OYP
Type
protein
Length
1,356 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
SO4
Pockets
11 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FRibonuclease pH (EC 2.7.7.56)protein22634% helix, 31% strandP28619

Ligands and binding sites

  • 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13590.630.7937SO4
23090.630.8041empty
33560.630.7944SO4
43420.620.7939SO4
53810.610.7739SO4

Interfaces

6 interfaces between chains.

  • A–B · 1389 Ų buried · 29 hydrogen bonds · protein-protein
  • E–F · 1348 Ų buried · 26 hydrogen bonds · protein-protein
  • C–D · 1269 Ų buried · 19 hydrogen bonds · protein-protein
  • D–E · 462 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 449 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 1OYP · 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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