- PDB-4lgk: X-ray structure of the adduct between hen egg white lysozyme and ... -
+
Open data
ID or keywords:
Loading...
-
Basic information
Entry
Database: PDB / ID: 4lgk
Title
X-ray structure of the adduct between hen egg white lysozyme and Au2Phen, a dinuclear gold(III) complex with -dioxo bridges linking the two metal centers
Components
Lysozyme C
Keywords
HYDROLASE
Function / homology
Function and homology information
Lactose synthesis / Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium ...Lactose synthesis / Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / defense response to Gram-negative bacterium / killing of cells of another organism / defense response to Gram-positive bacterium / defense response to bacterium / endoplasmic reticulum / extracellular space / identical protein binding / cytoplasm Similarity search - Function
Lysozyme - #10 / Glycoside hydrolase, family 22, lysozyme / Glycoside hydrolase family 22 domain / Glycosyl hydrolases family 22 (GH22) domain signature. / Glycoside hydrolase, family 22 / C-type lysozyme/alpha-lactalbumin family / Glycosyl hydrolases family 22 (GH22) domain profile. / Alpha-lactalbumin / lysozyme C / Lysozyme / Lysozyme-like domain superfamily ...Lysozyme - #10 / Glycoside hydrolase, family 22, lysozyme / Glycoside hydrolase family 22 domain / Glycosyl hydrolases family 22 (GH22) domain signature. / Glycoside hydrolase, family 22 / C-type lysozyme/alpha-lactalbumin family / Glycosyl hydrolases family 22 (GH22) domain profile. / Alpha-lactalbumin / lysozyme C / Lysozyme / Lysozyme-like domain superfamily / Orthogonal Bundle / Mainly Alpha Similarity search - Domain/homology
Mass: 18.015 Da / Num. of mol.: 167 / Source method: isolated from a natural source / Formula: H2O
Nonpolymer details
THE GOLD COMPOUND FORMING HEWL ADDUCT UNDERGOES EXTENSIVE DEGRADATION UPON REACTION WITH THIS ...THE GOLD COMPOUND FORMING HEWL ADDUCT UNDERGOES EXTENSIVE DEGRADATION UPON REACTION WITH THIS PROTEIN. THERE IS NO EVIDENCE OF THE PRESENCE OF THE ORIGINAL METAL LIGANDS FROM THE CRYSTAL STRUCTURE. THE STRUCTURE OF THE DINUCLEAR GOLD(III) COMPOUND IS COMPLETELY LOST AND THE METAL IS REDUCED OWING TO THE APPRECIABLE OXIDISING CHARACTER OF THESE GOLD(III) CENTERS. IT FOLLOWS THAT PROTEIN IS BOUND TO GOLD IN THE OXIDATION STATE +1 INDEPENDENTLY OF THE NATURE OF THE STARTING COMPOUND, AS DOCUMENTED BY ITS LINEAR COORDINATION.
-
Experimental details
-
Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
-
Sample preparation
Crystal
Density Matthews: 1.95 Å3/Da / Density % sol: 36.76 %