1HEL: Hen egg white lysozyme

Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme. Determined by X-ray diffraction at 1.7 Å resolution. Released 31 Oct 1993.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Gallus gallus
Chains
1
Atoms
1,186
Mol. weight
14.33 kDa
Released
31 Oct 1993

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

Secondary structure: helices and β-sheets

1HEL contains 7 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: 7 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand211
α-helix5-1410
β-strand2012
β-strand2312
α-helix25-3612
β-strand3911
β-strand43-4533
β-strand51-5333
β-strand58-5923
β-strand6514
β-strand7914
α-helix80-845
α-helix89-10012
α-helix104-1074
α-helix109-1146
α-helix120-1245

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Hen egg white lysozymeAprotein129Gallus gallusP00698 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1HEL_1 HEN EGG WHITE LYSOZYME (chains A)
KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINS
RWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDV
QAWIRGCRL

Primary citation

Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme. Wilson, K.P., Malcolm, B.A., Matthews, B.W. J Biol Chem (1992) 267:10842-10849. PubMed

Other PDB entries of the same protein (UniProt P00698 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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