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Crystallographic refinement of human serum retinol binding protein at 2 ångströms resolution

Analyse Crystallographic refinement of human serum retinol binding protein at 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1RBP
Type
protein
Length
174 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Plasma retinol-binding protein precursor
UniProt
P02753
Ligands
RTL
Pockets
2 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 47% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APlasma retinol-binding protein precursorprotein1749% helix, 47% strandP02753

Ligands and binding sites

  • RTL · Retinol · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12000.810.9529RTL
2550.290.7415empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1RBP · Crystallographic refinement of human serum retinol binding protein at 2 ångströms… · the same entry in another collection · chain A against A, TM-score 1.00
  • P02753 · AlphaFold monomer V2.0 prediction for retinol-binding protein 4 (P02753) · a predicted model of the same protein · chain A against A, TM-score 0.99

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