› 1jkb

X-ray diffraction
1.66Å resolution

HUMAN LYSOZYME MUTANT WITH GLU 35 REPLACED BY ALA

Released:
DOI: 10.2210/pdb1jkb/pdb
PDB entry 1jkb coloured by chain, front view.
PDB entry 1jkb coloured by chain, side view.
PDB entry 1jkb coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Importance of van der Waals contact between Glu 35 and Trp 109 to the catalytic action of human lysozyme.
Muraki M, Goda S, Nagahora H, Harata K
Protein Sci 6 473-6 (1997)
PMID: 9041653

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 Chain: A
Molecule details ›
Chain: A
Length: 130 amino acids
Theoretical weight: 14.66 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
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

1 bound ligand:
Ligand NO3 2 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P212121
Unit cell:
a: 56.95Å b: 60.97Å c: 33.16Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 0.202
Expression system: Saccharomyces cerevisiae

Quick links

Citations

7 citation in other articles

Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme.
Morozova-Roche et al. (1999)
6 more

1 mention without citation

Efficient structure-factor modeling for crystals with multiple components.
Afonine et al. (2023)