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Crystal structure of the R132K:R111L:T54E mutant of cellular retinoic acid-binding protein II at 1.85 angstrom resolution

Analyse Crystal structure of the R132K:R111L:T54E mutant of cellular retinoic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FEL
Type
protein
Length
274 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.85
Source
Homo sapiens
Molecule
Cellular retinoic acid-binding protein 2
UniProt
P29373
Pockets
2 · best druggability 0.79

Structure

x-ray diffraction · resolution 1.85 · 1 distinct chain · 12% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCellular retinoic acid-binding protein 2protein13712% helix, 55% strandP29373

Ligands and binding sites

  • B3P · 2-[3-(2-hydroxy-1,1-dihydroxymethyl-ethylamino)-propylamino]-2-hydroxymethyl-propane-1,3-diol · additive · 3 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14060.790.8842B3P
26330.740.8157B3P

Interfaces

1 interface between chains.

  • A–B · 34 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 3FEL · Crystal structure of the R132K:R111L:T54E mutant of cellular retinoic acid-binding… · the same entry in another collection · chain A against A, TM-score 1.00
  • P29373 · AlphaFold monomer V2.0 prediction for cellular retinoic acid-binding protein 2 (P29373) · a predicted model of the same protein · chain A against A, TM-score 0.98

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