› 2vb1

X-ray diffraction
0.65Å resolution

HEWL at 0.65 angstrom resolution

Released:
DOI: 10.2210/pdb2vb1/pdb
PDB entry 2vb1 coloured by chain, front view.
PDB entry 2vb1 coloured by chain, side view.
PDB entry 2vb1 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Triclinic lysozyme at 0.65 A resolution.
Wang J, Dauter M, Alkire R, Joachimiak A, Dauter Z
Acta Crystallogr D Biol Crystallogr 63 1254-68 (2007)
PMID: 18084073

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 Chain: A
Molecule details ›
Chain: A
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

3 bound ligands:
Ligand ACT 1 x ACT
Ligand EDO 3 x EDO
Ligand NO3 9 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 27.07Å b: 31.25Å c: 33.76Å
α: 87.98° β: 108° γ: 112.11°
R-values:
R R work R free
0.084 not available 0.095

Quick links

Citations

3 review citations

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

63 mentions without citation

Fidelity at the molecular level: lessons from protein synthesis.
Zaher et al. (2009)
62 more