3FE0: Wild type human lysozyme in D2O

X-ray crystal structure of wild type human lysozyme in D2O. Determined by X-ray diffraction at 1.5 Å resolution. Released 8 Dec 2009.

Method
X-ray diffraction
Resolution
1.5 Å
Organism
Homo sapiens
Chains
1
Atoms
1,167
Mol. weight
14.72 kDa
Released
8 Dec 2009

Explore 3FE0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3FE0 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
Lysozyme CAprotein130Homo sapiensP61626 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3FE0_1 Lysozyme C (chains A)
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQIN
SRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRD
VRQYVQGCGV

Primary citation

Site-specific softening of peptide bonds by localized deuterium observed by neutron crystallography of human lysozyme hydrogen. Chiba-Kamoshida, K., Matsui, T., Chatake, T. et al. To be published.

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

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