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Crystal structure of the E3 ubiquitin ligase ravn from legionella pneumophila

Analyse Crystal structure of the E3 ubiquitin ligase ravn from legionella pneumophila in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MIY
Type
protein
Length
372 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin ligase ravn
EC
6.3.2.19
UniProt
A0A130MLL2
Ligands
NA, SO4
Pockets
5 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 24% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin ligase ravn (EC 6.3.2.19)protein12724% helix, 26% strandA0A130MLL2
BE3 ubiquitin ligase ravn (EC 6.3.2.19)protein12327% helix, 28% strandA0A130MLL2
CE3 ubiquitin ligase ravn (EC 6.3.2.19)protein12220% helix, 30% strandA0A130MLL2

Ligands and binding sites

  • NA · Sodium ion · metal · 4 copies · chains A, C
  • SO4 · Sulfate ion · ion · 13 copies · chains A, B, C
  • EDO · 1,2-ethanediol · additive · 5 copies · chains A, B, 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12780.590.7827EDO
21490.460.7625NA
3580.450.8418empty
4510.390.8117empty
5610.380.7918empty

Interfaces

3 interfaces between chains.

  • A–C · 971 Ų buried · 8 hydrogen bonds · protein-protein
  • B–C · 527 Ų buried · 5 hydrogen bonds · protein-protein
  • A–B · 365 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 5MIY · Crystal structure of the E3 ubiquitin ligase RavN from Legionella pneumophila · the same entry in another collection · chain A against A, TM-score 1.00

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