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Ruva from mycobacterium tuberculosis

Analyse Ruva from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2H5X
Type
protein
Length
730 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Holliday junction ATP-dependent DNA helicase ruva
EC
3.6.1.-
UniProt
P66744
Pockets
8 · best druggability 0.83

Structure

x-ray diffraction · 4 distinct chains · 47% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHolliday junction ATP-dependent DNA helicase ruva (EC 3.6.1.-)protein18348% helix, 22% strandP66744
BHolliday junction ATP-dependent DNA helicase ruva (EC 3.6.1.-)protein18347% helix, 22% strandP66744
CHolliday junction ATP-dependent DNA helicase ruva (EC 3.6.1.-)protein18248% helix, 23% strandP66744
DHolliday junction ATP-dependent DNA helicase ruva (EC 3.6.1.-)protein18246% helix, 23% strandP66744

Ligands and binding sites

  • GOL · Glycerol · additive · 4 copies · chains A, B, C, D

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
11870.830.9632empty
2580.650.9419empty
34410.620.7651empty
43540.590.7644empty
53570.580.7647empty

Interfaces

6 interfaces between chains.

  • A–B · 1199 Ų buried · 11 hydrogen bonds · protein-protein
  • C–D · 1192 Ų buried · 15 hydrogen bonds · protein-protein
  • A–D · 1186 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 1167 Ų buried · 10 hydrogen bonds · protein-protein
  • A–C · 26 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2H5X · RuvA from Mycobacterium tuberculosis · the same entry in another collection · chain A against A, TM-score 1.00

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