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- PDB-8lyz: AN X-RAY STUDY OF THE STRUCTURE AND BINDING PROPERTIES OF IODINE-... -

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Entry
Database: PDB / ID: 8lyz
TitleAN X-RAY STUDY OF THE STRUCTURE AND BINDING PROPERTIES OF IODINE-INACTIVATED LYSOZYME
ComponentsHEN EGG WHITE LYSOZYME
KeywordsHYDROLASE (O-GLYCOSYL)
Function / homology
Function and homology information


Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / defense response to bacterium ...Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to Gram-negative bacterium / 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
Biological speciesGallus gallus (chicken)
MethodX-RAY DIFFRACTION / Resolution: 2.5 Å
AuthorsBeddell, C.R. / Blake, C.C.F. / Oatley, S.J.
Citation
Journal: J.Mol.Biol. / Year: 1975
Title: An x-ray study of the structure and binding properties of iodine-inactivated lysozyme.
Authors: Beddell, C.R. / Blake, C.C. / Oatley, S.J.
#1: Journal: J.Mol.Biol. / Year: 1974
Title: Real-Space Refinement of the Structure of Hen Egg-White Lysozyme
Authors: Diamond, R.
#2: Journal: Lysozyme / Year: 1974
Title: Crystallographic Studies of Lysozyme and its Interactions with Inhibitors and Substrates
Authors: Phillips, D.C.
#3: Journal: The Enzymes,Third Edition / Year: 1972
Title: Vertebrate Lysozymes
Authors: Imoto, T. / Johnson, L.N. / North, A.C.T. / Phillips, D.C. / Rupley, J.A.
#4: Journal: J.Mol.Biol. / Year: 1974
Title: Energy Refinement of Hen Egg-White Lysozyme
Authors: Levitt, M.
#5: Journal: J.Mol.Biol. / Year: 1974
Title: Crystal Structure of a Lysozyme-Tetrasaccharide Lactone Complex
Authors: Ford, L.O. / Johnson, L.N. / Machin, P.A. / Phillips, D.C. / Tjian, R.
#6: Journal: Proc.R.Soc.London,Ser.B / Year: 1967
Title: On the Conformation of the Hen Egg-White Lysozyme Molecule
Authors: Blake, C.C.F. / Mair, G.A. / North, A.C.T. / Phillips, D.C. / Sarma, V.R.
#7: Journal: Proc.R.Soc.London,Ser.B / Year: 1967
Title: Crystallographic Studies of the Activity of Hen Egg-White Lysozyme
Authors: Blake, C.C.F. / Johnson, L.N. / Mair, G.A. / North, A.C.T. / Phillips, D.C. / Sarma, V.R.
#8: Journal: Sci.Am. / Year: 1966
Title: The Three-Dimensional Structure of an Enzyme Molecule
Authors: Phillips, D.C.
#9: Journal: Nature / Year: 1965
Title: Structure of Hen Egg-White Lysozyme, a Three-Dimensional Fourier Synthesis at 2 Angstroms Resolution
Authors: Blake, C.C.F. / Koenig, D.F. / Mair, G.A. / North, A.C.T. / Phillips, D.C. / Sarma, V.R.
#10: Journal: Nature / Year: 1965
Title: Structure of Some Crystalline Lysozyme-Inhibitor Complexes Determined by X-Ray Analysis at 6 Angstroms Resolution
Authors: Johnson, L.N. / Phillips, D.C.
#11: Journal: Atlas of Macromolecular Structure on Microfiche / Year: 1976
#12: Journal: Atlas of Protein Sequence and Structure (Data Section)
Year: 1972
History
DepositionSep 16, 1977Processing site: BNL
Revision 1.0Oct 24, 1977Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HEN EGG WHITE LYSOZYME


Theoretical massNumber of molelcules
Total (without water)14,3311
Polymers14,3311
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)79.100, 79.100, 37.900
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein HEN EGG WHITE LYSOZYME


Mass: 14331.160 Da / Num. of mol.: 1
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: 2.07 Å3/Da / Density % sol: 40.52 %
Crystal grow
*PLUS
Method: other / Details: Blake, C.C.F., (1965) Nature, 206, 757.

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Data collection

Reflection
*PLUS
Highest resolution: 2.5 Å

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Processing

RefinementHighest resolution: 2.5 Å
Refinement stepCycle: LAST / Highest resolution: 2.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1000 0 0 0 1000

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