› 1ckg

X-ray diffraction
2.2Å resolution

T52V MUTANT HUMAN LYSOZYME

Released:
DOI: 10.2210/pdb1ckg/pdb
PDB entry 1ckg coloured by chain, front view.
PDB entry 1ckg coloured by chain, side view.
PDB entry 1ckg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Contribution of intra- and intermolecular hydrogen bonds to the conformational stability of human lysozyme(,).
Takano K, Yamagata Y, Funahashi J, Hioki Y, Kuramitsu S, Yutani K
Biochemistry 38 12698-708 (1999)
PMID: 10504240

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158309 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chains: A, B
Molecule details ›
Chains: A, B
Length: 130 amino acids
Theoretical weight: 14.72 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 65.257Å b: 106.667Å c: 39.542Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.166 not available
Expression system: Saccharomyces cerevisiae

Quick links

Citations

2 review citations

Do all backbone polar groups in proteins form hydrogen bonds?
Fleming et al. (2005)
1 more

1 mention without citation

Organization and evolution of the chalcone synthase gene family in bread wheat and relative species.
Glagoleva et al. (2019)