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Bh-RNASEH:2'-sme-DNA complex

Analyse Bh-RNASEH:2'-sme-DNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4OPK
Type
protein + DNA
Length
290 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease H; 5'-D(*CP*GP*CP*GP*AP*AP*(USM)P*TP*CP*GP*CP*G)-3'
EC
3.1.26.4
UniProt
Q9KEI9
Pockets
5 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CRibonuclease H (EC 3.1.26.4)protein13335% helix, 26% strandQ9KEI9
B, D5'-D(*CP*GP*CP*GP*AP*AP*(USM)P*TP*CP*GP*CP*G)-3'dna12——

Ligands and binding sites

  • GOL · Glycerol · additive · 2 copies · chains A, C

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1700.440.8213empty
2640.430.8213empty
3560.320.7610empty
4550.320.7612GOL
5800.290.7219empty

Interfaces

3 interfaces between chains.

  • C–D · 324 Ų buried · 9 hydrogen bonds · protein-nucleic
  • A–B · 306 Ų buried · 6 hydrogen bonds · protein-nucleic
  • A–C · 108 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 modified (nucleotide modification).

Compared structures

  • 4OPK · Bh-RNaseH:2'-SMe-DNA complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9KEI9 · AlphaFold monomer V2.0 prediction for ribonuclease H (Q9KEI9) · a predicted model of the same protein · chain A against A, TM-score 0.99

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