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Crystal structure of cellular retinoic acid binding protein type II in complex with all-trans-retinoic acid at 1.48 ångströms resolution

Analyse Crystal structure of cellular retinoic acid binding protein type II in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FR3
Type
protein
Length
137 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cellular retinoic acid binding protein 2
UniProt
P29373
Ligands
REA
Pockets
1 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACellular retinoic acid binding protein 2protein13713% helix, 55% strandP29373

Ligands and binding sites

  • REA · Retinoic acid · ligand · chains A
  • ACT · Acetate ion · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13060.770.8941REA

Compared structures

  • 2FR3 · Crystal Structure of Cellular Retinoic Acid Binding Protein Type II in Complex with… · 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 0.99

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