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Structure of a bmi-1-RING1B polycomb group ubiquitin ligase complex

Analyse Structure of a bmi-1-RING1B polycomb group ubiquitin ligase complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2H0D
Type
protein
Length
197 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
B lymphoma mo-mlv insertion region; Ubiquitin ligase protein RING2
EC
6.3.2.-
UniProt
Q5T8Z3, Q99496
Ligands
ZN
Pockets
1 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AB lymphoma mo-mlv insertion regionprotein9744% helix, 15% strandQ5T8Z3
BUbiquitin ligase protein RING2 (EC 6.3.2.-)protein10030% helix, 17% strandQ99496

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1530.310.7615empty

Interfaces

1 interface between chains.

  • A–B · 2311 Ų buried · 33 hydrogen bonds · protein-protein

Compared structures

  • 2H0D · Structure of a Bmi-1-Ring1B Polycomb group ubiquitin ligase complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q99496 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RING2 (Q99496) · a predicted model of the same protein · chain B against A, TM-score 0.92

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