› 1lkr

X-ray diffraction
1.6Å resolution

MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE

Released:
DOI: 10.2210/pdb1lkr/pdb
PDB entry 1lkr coloured by chain, front view.
PDB entry 1lkr coloured by chain, side view.
PDB entry 1lkr coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Structures of monoclinic lysozyme iodide at 1.6 A and of triclinic lysozyme nitrate at 1.1 A.
Steinrauf LK
Acta Crystallogr D Biol Crystallogr 54 767-80 (1998)
PMID: 9757091

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-132831 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysozyme C Chains: A, B
Molecule details ›
Chains: A, B
Length: 129 amino acids
Theoretical weight: 14.33 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P00698 (Residues: 19-147; Coverage: 100%)
Gene name: LYZ
Sequence domains: C-type lysozyme/alpha-lactalbumin family
Structure domains: Lysozyme

Ligands and Environments

1 bound ligand:
Ligand IOD 17 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 27.894Å b: 63.153Å c: 60.227Å
α: 90° β: 90.12° γ: 90°
R-values:
R R work R free
0.106 not available 0.14

Quick links

Citations

2 review citations

Why continuum electrostatics theories cannot explain biological structure, polyelectrolytes or ionic strength effects in ion-protein interactions.
Collins KD. (2012)
1 more

1 mention without citation

Chemical conversion of cisplatin and carboplatin with histidine in a model protein crystallized under sodium iodide conditions.
Tanley et al. (2014)