1BRQ: Retinol binding protein

Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 Å resolution. Determined by X-ray diffraction at 2.5 Å resolution. Released 31 Jan 1994.

Method
X-ray diffraction
Resolution
2.5 Å
Organism
Homo sapiens
Chains
1
Atoms
1,463
Mol. weight
20.98 kDa
Released
31 Jan 1994

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

Secondary structure: helices and β-sheets

1BRQ contains 3 α-helices and 11 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: 3 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand511
α-helix6-83
α-helix17-204
β-strand22-3092
β-strand42-4872
β-strand52-62112
β-strand68-78112
β-strand85-9282
β-strand99-109112
β-strand114-123102
β-strand12811
β-strand129-138102
α-helix146-15813
β-strand166-16722

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Retinol binding proteinAprotein182Homo sapiensP02753 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1BRQ_1 RETINOL BINDING PROTEIN (chains A)
ERDCRVSSFRVKENFDKARFSGTWYAMAKKDPEGLFLQDNIVAEFSVDETGQMSATAKGR
VRLLNNWDVCADMVGTFTDTEDPAKFKMKYWGVASFLQKGNDDHWIVDTDYDTYAVQYSC
RLLNLDGTCADSYSFVFSRDPNGLPPEAQKIVRQRQEELCLARQYRLIVHNGYCDGRSER
NL

Primary citation

Crystal structure of the trigonal form of human plasma retinol-binding protein at 2.5 A resolution. Zanotti, G., Ottonello, S., Berni, R. et al. J Mol Biol (1993) 230:613-624. DOI 10.1006/jmbi.1993.1173 · PubMed

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

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