Structural changes of the active site cleft and different saccharide binding modes in human lysozyme co-crystallized with hexa-N-acetyl-chitohexaose at PH 4.0. Determined by X-ray diffraction at 1.5 Å resolution. Released 20 Apr 1995.
Explore 1LZR in 3D Show helices and sheets RCSB PDB PDBe
1LZR 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 | 43-46 | 4 | 3 |
| β-strand | 51-54 | 4 | 3 |
| β-strand | 59-60 | 2 | 3 |
| β-strand | 66 | 1 | 4 |
| β-strand | 80 | 1 | 4 |
| α-helix | 81-85 | 5 | |
| α-helix | 90-100 | 11 | |
| α-helix | 105-108 | 4 | |
| α-helix | 110-115 | 6 | |
| α-helix | 122-124 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human lysozyme | A | protein | 130 | Homo sapiens | P61626 (AlphaFold model) |
>1LZR_1 HUMAN LYSOZYME (chains A) KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQIN SRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRD VRQYVQGCGV
Structural changes of active site cleft and different saccharide binding modes in human lysozyme co-crystallized with hexa-N-acetyl-chitohexaose at pH 4.0. Song, H., Inaka, K., Maenaka, K. et al. J Mol Biol (1994) 244:522-540. DOI 10.1006/jmbi.1994.1750 · PubMed
Other PDB entries of the same protein (UniProt P61626 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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