1REX: Native human lysozyme

Native human lysozyme. Determined by X-ray diffraction at 1.5 Å resolution. Released 12 Feb 1997.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Homo sapiens
Chains
1
Atoms
1,135
Mol. weight
14.72 kDa
Released
12 Feb 1997

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

Secondary structure: helices and β-sheets

1REX 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-strand43-4643
β-strand51-5443
β-strand59-6023
β-strand6614
β-strand8014
α-helix81-855
α-helix90-9910
α-helix105-1084
α-helix110-1156
α-helix122-1243

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
LysozymeAprotein130Homo sapiensP61626 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1REX_1 LYSOZYME (chains A)
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQIN
SRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRD
VRQYVQGCGV

Primary citation

Origin of carbohydrate recognition specificity of human lysozyme revealed by affinity labeling. Muraki, M., Harata, K., Sugita, N. et al. Biochemistry (1996) 35:13562-13567. DOI 10.1021/bi9613180 · PubMed

Other PDB entries of the same protein (UniProt P61626 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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