› 1rem

X-ray diffraction
2.1Å resolution

HUMAN LYSOZYME WITH MAN-B1,4-GLCNAC COVALENTLY ATTACHED TO ASP53

Released:
DOI: 10.2210/pdb1rem/pdb
PDB entry 1rem coloured by chain, front view.
PDB entry 1rem coloured by chain, side view.
PDB entry 1rem coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray structure of human lysozyme labelled with 2',3'-epoxypropyl beta-glycoside of man-beta1,4-GlcNAc. Structural change and recognition specificity at subsite B.
Muraki M, Harata K, Sugita N, Sato Ki
Acta Crystallogr D Biol Crystallogr 54 834-43 (1998)
PMID: 9757098

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
Macromolecules (2 distinct):
Lysozyme C Chain: A
Molecule details ›
Chain: A
Length: 130 amino acids
Theoretical weight: 14.72 KDa
Source organism: Homo sapiens
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

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
2 bound ligands:
Ligand NO3 1 x NO3
Ligand PGR 1 x PGR
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 36.39Å b: 116.38Å c: 30.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 0.248

Quick links

Citations

1 citations in other articles

The CH/π hydrogen bond in chemistry. Conformation, supramolecules, optical resolution and interactions involving carbohydrates.
Nishio M. (2011)

1 mention without citation

Crystallographic refinement of ligand complexes.
Kleywegt GJ. (2007)