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Ligands
Code Name Style Show Link
CL Chloride ion
NA Sodium ion
Non-standard Residues
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Glycosylation
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Code : 193L   PDBj   RCSB PDB   PDBe
Header : HYDROLASE (O-GLYCOSYL)
Title : THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME
Release Data : 1995-12-07
Compound :
mol_id molecule chains
1 LYSOZYME A
Source :
mol_id organism_scientific organism_common
1 Gallus gallus  (taxid:9031) Chicken
cellular_location: EGG WHITE
Authors : Vaney, M.C., Maignan, S., Ries-Kautt, M., Ducruix, A.
Keywords : HYDROLASE (O-GLYCOSYL)
Exp. method : X-RAY DIFFRACTION ( 1.33 Å )
Citation :

High-resolution structure (1.33 A) of a HEW lysozyme tetragonal crystal grown in the APCF apparatus. Data and structural comparison with a crystal grown under microgravity from SpaceHab-01 mission.

Vaney, M.C.,Maignan, S.,Ries-Kautt, M.  et al.
(1996)  Acta Crystallogr.,Sect.D  52 : 505 - 517

PubMed: 15299672
DOI: 10.1107/S090744499501674X

Effect of Microgravity on Rate of Nucleation, Size and Quality of Lysozyme Crystals Grown in the Advanced Protein Crystallization Facility on Spacehab-01

Ries-Kautt, M.M.,Broutin, I.,Ducruix, A.F.  et al.
To be Published 

Thermal Expansion of Hen-Egg-White Lysozyme. Comparison of the 1.9 Angstroms Resolution Structures of the Tetragonal Form of the Enzyme at 100K and 298K

Young, A.C.M.,Tilton, R.F.,Dewan, J.C.
(1994)  J.Mol.Biol.  235 : 302

Experiment and Equipment for Protein Crystallization in Microgram Facilities

Bosch, R.,Lautenschlager, P.,Potthast, L.  et al.
(1992)  J.Cryst.Growth  122 : 310

Chain : A
UniProt : P00698 (LYSC_CHICK)
Reaction: EC: Evidence:
Physiological Direction:
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. 3.2.1.17 -
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