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4J7V

Crystal structure of cross-linked hen egg white lysozyme soaked with 5mM [Ru(benzene)Cl2]2

Summary for 4J7V
Entry DOI10.2210/pdb4j7v/pdb
Related3W6A
DescriptorLysozyme C, CHLORIDE ION, SODIUM ION, ... (5 entities in total)
Functional Keywordshydrolase
Biological sourceGallus gallus (chicken)
Cellular locationSecreted: P00698
Total number of polymer chains1
Total formula weight14781.50
Authors
Tabe, H.,Abe, S.,Hikage, T.,Kitagawa, S.,Ueno, T. (deposition date: 2013-02-14, release date: 2014-02-19, Last modification date: 2024-11-20)
Primary citationTabe, H.,Abe, S.,Hikage, T.,Kitagawa, S.,Ueno, T.
Porous protein crystals as catalytic vessels for organometallic complexes.
Chem Asian J, 9:1373-1378, 2014
Cited by
PubMed Abstract: Porous protein crystals, which are protein assemblies in the solid state, have been engineered to form catalytic vessels by the incorporation of organometallic complexes. Ruthenium complexes in cross-linked porous hen egg white lysozyme (HEWL) crystals catalyzed the enantioselective hydrogen-transfer reduction of acetophenone derivatives. The crystals accelerated the catalytic reaction and gave different enantiomers based on the crystal form (tetragonal or orthorhombic). This method represents a new approach for the construction of bioinorganic catalysts from protein crystals.
PubMed: 24677803
DOI: 10.1002/asia.201301347
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.54 Å)
Structure validation

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