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The interaction of N-ethyl retinamide with plasma retinol-binding protein (rbp) and the crystal structure of the retinoid-rbp complex at 1.9 ångströms resolution

Analyse The interaction of N-ethyl retinamide with plasma retinol-binding protein (rbp)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1ERB
Type
protein
Length
173 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Retinol binding protein
UniProt
P18902
Ligands
ETR
Pockets
1 · best druggability 0.82

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARetinol binding proteinprotein17312% helix, 47% strandP18902

Ligands and binding sites

  • ETR · N-ethyl retinamide · ligand · 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
12350.820.9430ETR

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1ERB · The interaction of N-ethyl retinamide with plasma retinol-binding protein (rbp) and the… · the same entry in another collection · chain A against A, TM-score 1.00
  • P18902 · AlphaFold monomer V2.0 prediction for retinol-binding protein 4 (P18902) · a predicted model of the same protein · chain A against A, TM-score 0.99

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