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Crystallographic studies on a family of cellular lipophilic transport proteins. refinement of P2 myelin protein and the structure determination and refinement of cellular retinol-binding protein in complex with all-trans-retinol

Analyse Crystallographic studies on a family of cellular lipophilic transport proteins.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1CRB
Type
protein
Length
134 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cellular retinol binding protein
UniProt
P02696
Ligands
RTL, CD
Pockets
1 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 54% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACellular retinol binding proteinprotein13411% helix, 54% strandP02696

Ligands and binding sites

  • RTL · Retinol · ligand · chains A
  • CD · Cadmium ion · metal · 2 copies · 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
12720.840.9535RTL

Compared structures

  • 1CRB · Crystallographic studies on a family of cellular lipophilic transport proteins.… · the same entry in another collection · chain A against A, TM-score 1.00
  • P02696 · AlphaFold monomer V2.0 prediction for retinol-binding protein 1 (P02696) · a predicted model of the same protein · chain A against A, TM-score 0.98

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