› 1jpo

X-ray diffraction
2.1Å resolution

LOW TEMPERATURE ORTHORHOMBIC LYSOZYME

Released:
DOI: 10.2210/pdb1jpo/pdb
PDB entry 1jpo coloured by chain, front view.
PDB entry 1jpo coloured by chain, side view.
PDB entry 1jpo coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Time-Resolved Biological and Perturbation Chemical Crystallography: Laue and Monochromatic Developments
Bradbrook S, Deacon A, Habash J, Helliwell JR, Helliwell M, Nieh YP, Snell EH, Trapani G, Thompson AW, Campbell JW, Allinson NM, Moon K, Ursby T, Wulff M
Time-Resolved Electron and X-Ray Diffraction; 13-14 July 1995, San Diego, California (in: Proc.Spie-Int.Soc.Opt.Eng., V.2521) 160- (1995)

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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 59.4Å b: 68.57Å c: 30.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 not available

Quick links

Citations

1 mention without citation

Peripheral regions of natural hammerhead ribozymes greatly increase their self-cleavage activity.
De la Peña et al. (2003)