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Structure of D132N T4 RNase H in the presence of divalent magnesium

Analyse Structure of D132N T4 RNase H in the presence of divalent magnesium in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3H8W
Type
protein
Length
284 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribonuclease H
EC
3.1.26.4
UniProt
P13319
Pockets
4 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 53% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibonuclease H (EC 3.1.26.4)protein28453% helix, 10% strandP13319

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12310.590.8037empty
2640.380.7916empty
3870.350.7513empty
4540.320.7613empty

Compared structures

  • 3H8W · Structure of D132N T4 RNase H in the presence of divalent magnesium · the same entry in another collection · chain A against A, TM-score 1.00

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