1B8E: Protein

High resolution crystal structure of the bovine beta-lactoglobulin (isoforms a and B) in orthorombic space group. Determined by X-ray diffraction at 1.95 Å resolution. Released 2 May 2001.

Method
X-ray diffraction
Resolution
1.95 Å
Organism
Bos taurus
Chains
1
Atoms
1,301
Mol. weight
18.3 kDa
Released
2 May 2001

Explore 1B8E in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1B8E contains 6 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: 6 helices, 11 β-strands

ElementResiduesLengthSheet
α-helix3-53
α-helix71
α-helix12-154
β-strand17-1821
β-strand20-2672
α-helix29-324
β-strand42-4871
β-strand54-6291
β-strand65-7391
β-strand74-7522
β-strand81-8442
β-strand90-9782
β-strand102-10982
β-strand116-12382
α-helix131-1399
α-helix140-1423
β-strand147-15042

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (beta-lactoglobulin)Aprotein162Bos taurusP02754 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1B8E_1 PROTEIN (BETA-LACTOGLOBULIN) (chains A)
LIVTQTMKGLDIQKVAGTWYSLAMAASDISLLDAQSAPLRVYVEELKPTPEGDLEILLQK
WENGECAQKKIIAEKTKIPAVFKIDALNENKVLVLDTDYKKYLLFCMENSAEPEQSLACQ
CLVRTPEVDDEALEKFDKALKALPMHIRLSFNPTQLEEQCHI

Primary citation

Crystal structures of bovine beta-lactoglobulin in the orthorhombic space group C222(1). Structural differences between genetic variants A and B and features of the Tanford transition. Oliveira, K.M., Valente-Mesquita, V.L., Botelho, M.M. et al. Eur J Biochem (2001) 268:477-483. PubMed

Other PDB entries of the same protein (UniProt P02754 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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