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Crystal structure of E.COLI RNase hi active site mutant (K87A/H124A)

Analyse Crystal structure of E.COLI RNase hi active site mutant (K87A/H124A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1WSJ
Type
protein
Length
1,210 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease hi
EC
3.1.26.4
UniProt
P0A7Y4
Pockets
9 · best druggability 0.44

Structure

x-ray diffraction · 7 distinct chains · 36% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibonuclease hi (EC 3.1.26.4)protein15535% helix, 31% strandP0A7Y4
B, ERibonuclease hi (EC 3.1.26.4)protein15336% helix, 31% strandP0A7Y4
CRibonuclease hi (EC 3.1.26.4)protein14938% helix, 31% strandP0A7Y4
DRibonuclease hi (EC 3.1.26.4)protein14937% helix, 32% strandP0A7Y4
FRibonuclease hi (EC 3.1.26.4)protein15235% helix, 32% strandP0A7Y4
GRibonuclease hi (EC 3.1.26.4)protein14838% helix, 34% strandP0A7Y4
HRibonuclease hi (EC 3.1.26.4)protein15135% helix, 33% strandP0A7Y4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1640.440.8214empty
21930.440.7326empty
3570.400.8113empty
4580.360.7913empty
5760.360.7613empty

Interfaces

3 interfaces between chains.

  • B–E · 135 Ų buried · 2 hydrogen bonds · protein-protein
  • C–F · 59 Ų buried · 0 hydrogen bonds · protein-protein
  • A–H · 47 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1WSJ · Crystal structure of E.coli RNase HI active site mutant (K87A/H124A) · the same entry in another collection · chain G against G, TM-score 1.00
  • P0A7Y4 · AlphaFold monomer V2.0 prediction for ribonuclease hi (P0A7Y4) · a predicted model of the same protein · chain C against A, TM-score 0.99

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