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Structure of RLD2 brx domain bound to LZY3 ccl motif

Analyse Structure of RLD2 brx domain bound to LZY3 ccl motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6L0W
Type
protein
Length
154 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RLD2; NGR2
UniProt
F4K0X5, Q5XVG3
Pockets
1 · best druggability 0.29

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CRLD2protein6130% helix, 34% strandF4K0X5
B, DNGR2protein160% helix, 50% strandQ5XVG3

Ligands and binding sites

  • FLC · Citrate anion · additive · 2 copies · chains A, C
  • EDO · 1,2-ethanediol · additive · chains A, C

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
1540.290.7516empty

Interfaces

4 interfaces between chains.

  • A–B · 770 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 768 Ų buried · 12 hydrogen bonds · protein-protein
  • A–C · 443 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 35 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 6L0W · Structure of RLD2 BRX domain bound to LZY3 CCL motif · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5XVG3 · AlphaFold monomer V2.0 prediction for protein lazy 4 (Q5XVG3) · a predicted model of the same protein · chain B against A, TM-score 0.24

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