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- PDB-1lzh: THE STRUCTURES OF THE MONOCLINIC AND ORTHORHOMBIC FORMS OF HEN EG... -

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Basic information

Entry
Database: PDB / ID: 1lzh
TitleTHE STRUCTURES OF THE MONOCLINIC AND ORTHORHOMBIC FORMS OF HEN EGG-WHITE LYSOZYME AT 6 ANGSTROMS RESOLUTION.
ComponentsHEN EGG WHITE LYSOZYME
KeywordsHYDROLASE (O-GLYCOSYL)
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
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 speciesGallus gallus (chicken)
MethodX-RAY DIFFRACTION / Resolution: 6 Å
AuthorsArtymiuk, P.J. / Blake, C.C.F. / Rice, D.W. / Wilson, K.S.
CitationJournal: Acta Crystallogr.,Sect.B / Year: 1982
Title: The Structures of the Monoclinic and Orthorhombic Forms of Hen Egg-White Lysozyme at 6 Angstroms Resolution.
Authors: Artymiuk, P.J. / Blake, C.C.F. / Rice, D.W. / Wilson, K.S.
History
DepositionJun 29, 1981Processing site: BNL
Revision 1.0Sep 28, 1981Provider: repository / Type: Initial release
Revision 1.1Mar 3, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: HEN EGG WHITE LYSOZYME
B: HEN EGG WHITE LYSOZYME


Theoretical massNumber of molelcules
Total (without water)28,6622
Polymers28,6622
Non-polymers00
Water00
1
A: HEN EGG WHITE LYSOZYME


Theoretical massNumber of molelcules
Total (without water)14,3311
Polymers14,3311
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: HEN EGG WHITE LYSOZYME


Theoretical massNumber of molelcules
Total (without water)14,3311
Polymers14,3311
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)28.120, 63.610, 60.520
Angle α, β, γ (deg.)90.00, 91.05, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.97571, -0.2076, 0.06998), (0.2156, 0.96659, -0.13867), (-0.03885, 0.15039, 0.98786)
Vector: -14.1959, 0.72997, -30.52292)

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Components

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


Mass: 14331.160 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / References: UniProt: P00698, lysozyme

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 1.89 Å3/Da / Density % sol: 34.85 %
Crystal grow
*PLUS
pH: 9.6 / Method: unknown
Details: taken from Steinrauf, L.K. (1959). Acta Cryst. 12, 77.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-ID
13 %(w/v)protein11
25 %sodium chloride11

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Processing

RefinementHighest resolution: 6 Å
Refinement stepCycle: LAST / Highest resolution: 6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms258 0 0 0 258
Refinement
*PLUS
Highest resolution: 6 Å
Solvent computation
*PLUS
Displacement parameters
*PLUS

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