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- PDB-1lz2: CRYSTALLOGRAPHIC STUDY OF TURKEY EGG-WHITE LYSOZYME AND ITS COMPL... -

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Basic information

Entry
Database: PDB / ID: 1lz2
TitleCRYSTALLOGRAPHIC STUDY OF TURKEY EGG-WHITE LYSOZYME AND ITS COMPLEX WITH A DISACCHARIDE
ComponentsTURKEY EGG WHITE LYSOZYME
KeywordsHYDROLASE (O-GLYCOSYL)
Function / homology
Function and homology information


glycosaminoglycan binding / 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 / extracellular space / identical protein binding / cytoplasm
Similarity search - Function
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-like domain superfamily
Similarity search - Domain/homology
Biological speciesMeleagris gallopavo (turkey)
MethodX-RAY DIFFRACTION / Resolution: 2.8 Å
AuthorsBott, R. / Sarma, R.
Citation
Journal: J.Mol.Biol. / Year: 1977
Title: Crystallographic study of turkey egg-white lysozyme and its complex with a disaccharide.
Authors: Sarma, R. / Bott, R.
#1: Journal: J.Mol.Biol. / Year: 1976
Title: Crystal Structure of Turkey Egg-White Lysozyme. Results of the Molecular Replacement Method at 5 Angstroms Resolution
Authors: Sarma, R. / Bott, R.
History
DepositionSep 21, 1981Processing site: BNL
Revision 1.0Dec 8, 1981Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 14, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: TURKEY EGG WHITE LYSOZYME


Theoretical massNumber of molelcules
Total (without water)14,2561
Polymers14,2561
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)71.000, 71.000, 84.600
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122

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Components

#1: Protein TURKEY EGG WHITE LYSOZYME / Coordinate model: Cα atoms only


Mass: 14256.119 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Meleagris gallopavo (turkey) / References: UniProt: P00703

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.16 Å3/Da / Density % sol: 43.02 %
Crystal grow
*PLUS
Method: other / Details: Bott, R., (1976) J. Mol. Biol., 106, 1037.

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Processing

RefinementHighest resolution: 2.8 Å
Refinement stepCycle: LAST / Highest resolution: 2.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms129 0 0 0 129
Refinement
*PLUS
Lowest resolution: 10 Å / Rfactor obs: 0.467
Solvent computation
*PLUS
Displacement parameters
*PLUS

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