› 1qsw

X-ray diffraction
1.85Å resolution

CRYSTAL STRUCTURE ANALYSIS OF A HUMAN LYSOZYME MUTANT W64C C65A

Released:
DOI: 10.2210/pdb1qsw/pdb
PDB entry 1qsw coloured by chain, front view.
PDB entry 1qsw coloured by chain, side view.
PDB entry 1qsw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of a mutant human lysozyme with a substituted disulfide bond.
Inaka K, Kanaya E, Kikuchi M, Miki K
Proteins 43 413-9 (2001)
PMID: 11340658

Function and Biology Details

Reaction catalysed: 
Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 130 amino acids
Theoretical weight: 14.61 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P61626 (Residues: 19-148; Coverage: 100%)
Gene names: LYZ, LZM
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P1
Unit cell:
a: 45.92Å b: 107.24Å c: 32.08Å
α: 98.59° β: 110.45° γ: 78.04°
R-values:
R R work R free
0.181 0.181 0.261

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Citations

1 citations in other articles

Identification and characterization of disulfide bonds in proteins and peptides from tandem MS data by use of the MassMatrix MS/MS search engine.
Xu et al. (2008)