1JSF: Lysozyme

Full-matrix least-squares refinement of human lysozyme. Determined by X-ray diffraction at 1.15 Å resolution. Released 29 Apr 1998.

Method
X-ray diffraction
Resolution
1.15 Å
Organism
Homo sapiens
Chains
1
Atoms
1,253
Mol. weight
15.15 kDa
Released
29 Apr 1998

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

Secondary structure: helices and β-sheets

1JSF 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-helix90-10011
α-helix105-1084
α-helix110-1156
α-helix122-1243

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
LysozymeAprotein130Homo sapiensP61626 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1JSF_1 LYSOZYME (chains A)
KVFERCELARTLKRLGMDGYRGISLANWMCLAKWESGYNTRATNYNAGDRSTDYGIFQIN
SRYWCNDGKTPGAVNACHLSCSALLQDNIADAVACAKRVVRDPQGIRAWVAWRNRCQNRD
VRQYVQGCGV

Primary citation

Full-matrix least-squares refinement of lysozymes and analysis of anisotropic thermal motion. Harata, K., Abe, Y., Muraki, M. Proteins (1998) 30:232-243. DOI 10.1002/(SICI)1097-0134(19980215)30:3<232::AID-PROT3>3.3.CO;2-B · 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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