› 4r6c

X-ray diffraction
1.7Å resolution

X-ray diffraction in temporally and spatially resolved biomolecular science: the X-ray crystal structure of hen egg white lysozyme cocrystallized with Ta6Br12 and then a crystal soaked in K2PtBr6

Released:
DOI: 10.2210/pdb4r6c/pdb
PDB entry 4r6c coloured by chain, front view.
PDB entry 4r6c coloured by chain, side view.
PDB entry 4r6c coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
X-ray diffraction in temporally and spatially resolved biomolecular science.
Helliwell JR, Brink A, Kaenket S, Starkey VL, Tanley SW
Faraday Discuss 177 429-41 (2015)
PMID: 25605312

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 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

5 bound ligands:
Ligand TBR 2 x TBR
Ligand 6BP 2 x 6BP
Ligand BR 1 x BR
Ligand CL 12 x CL
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: Cu FINE FOCUS
Spacegroup: P43212
Unit cell:
a: 79.07Å b: 79.07Å c: 37.235Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.18 0.23

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Citations

1 citations in other articles

Spatio-temporal resolution of primary processes of photosynthesis.
Junge W. (2015)