1RBP: Plasma retinol-binding protein precursor

Crystallographic refinement of human serum retinol binding protein at 2 Å resolution. Determined by X-ray diffraction at 2.0 Å resolution. Released 15 Jul 1991.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
1,582
Mol. weight
21.27 kDa
Ligands
RTL
Released
15 Jul 1991

Explore 1RBP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1RBP contains 2 α-helices and 9 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 2 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix6-83
β-strand22-3091
β-strand39-4791
β-strand53-63111
β-strand67-79131
β-strand85-9281
β-strand100-109101
β-strand114-123101
β-strand129-138101
α-helix146-15813
β-strand166-16721

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Plasma retinol-binding protein precursorAprotein182Homo sapiensP02753 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1RBP_1 PLASMA RETINOL-BINDING PROTEIN PRECURSOR (chains A)
ERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKGR
VRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSC
RLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYCDGRSER
NL

Ligands and cofactors

IDNameFormulaCopies
RTLRetinolC20 H30 O1

Primary citation

Crystallographic refinement of human serum retinol binding protein at 2A resolution. Cowan, S.W., Newcomer, M.E., Jones, T.A. Proteins (1990) 8:44-61. DOI 10.1002/prot.340080108 · PubMed

Other PDB entries of the same protein (UniProt P02753 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1RBP directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.