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.
Explore 1HEL in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2 | 1 | 1 |
| α-helix | 5-14 | 10 | |
| β-strand | 20 | 1 | 2 |
| β-strand | 23 | 1 | 2 |
| α-helix | 25-36 | 12 | |
| β-strand | 39 | 1 | 1 |
| β-strand | 43-45 | 3 | 3 |
| β-strand | 51-53 | 3 | 3 |
| β-strand | 58-59 | 2 | 3 |
| β-strand | 65 | 1 | 4 |
| β-strand | 79 | 1 | 4 |
| α-helix | 80-84 | 5 | |
| α-helix | 89-100 | 12 | |
| α-helix | 104-107 | 4 | |
| α-helix | 109-114 | 6 | |
| α-helix | 120-124 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Hen egg white lysozyme | A | protein | 129 | Gallus gallus | P00698 (AlphaFold model) |
>1HEL_1 HEN EGG WHITE LYSOZYME (chains A) KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINS RWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDV QAWIRGCRL
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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