› 5fcp

X-ray diffraction
1.55Å resolution

X-RAY STRUCTURE OF THE ADDUCT BETWEEN HEN EGG WHITE LYSOZYME AND CISPLATIN AT LONG INCUBATION TIMES

Released:
DOI: 10.2210/pdb5fcp/pdb
PDB entry 5fcp coloured by chain, front view.
PDB entry 5fcp coloured by chain, side view.
PDB entry 5fcp coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Effect of temperature on the interaction of cisplatin with the model protein hen egg white lysozyme.
Ferraro G, Pica A, Russo Krauss I, Pane F, Amoresano A, Merlino A
J Biol Inorg Chem 21 433-42 (2016)
PMID: 27040953

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

3 bound ligands:
Ligand GOL 2 x GOL
Ligand CPT 2 x CPT
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P43212
Unit cell:
a: 79.28Å b: 79.28Å c: 37.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.213

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Citations

15 citation in other articles

Protein metalation by metal-based drugs: X-ray crystallography and mass spectrometry studies.
Messori et al. (2017)
14 more