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PDBsum entry 2fbb

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protein ligands metals links
Hydrolase PDB id
2fbb

 

 

 

 

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Contents
Protein chain
129 a.a. *
Ligands
NO3 ×16
Metals
_NA ×5
Waters ×165
* Residue conservation analysis
PDB id:
2fbb
Name: Hydrolase
Title: Crystal structure analysis of hexagonal lysozyme
Structure: LysozymE C. Chain: a. Synonym: 1,4-beta-n-acetylmuramidasE C, allergen gal d 4, gal d iv. Ec: 3.2.1.17
Source: Gallus gallus. Chicken. Organism_taxid: 9031
Resolution:
1.46Å     R-factor:   0.183     R-free:   0.198
Authors: C.Brinkmann,M.S.Weiss,E.Weckert
Key ref:
C.Brinkmann et al. (2006). The structure of the hexagonal crystal form of hen egg-white lysozyme. Acta Crystallogr D Biol Crystallogr, 62, 349-355. PubMed id: 16552135 DOI: 10.1107/S0907444906000825
Date:
09-Dec-05     Release date:   28-Mar-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P00698  (LYSC_CHICK) -  Lysozyme C from Gallus gallus
Seq:
Struc:
147 a.a.
129 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.17  - lysozyme.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

 

 
DOI no: 10.1107/S0907444906000825 Acta Crystallogr D Biol Crystallogr 62:349-355 (2006)
PubMed id: 16552135  
 
 
The structure of the hexagonal crystal form of hen egg-white lysozyme.
C.Brinkmann, M.S.Weiss, E.Weckert.
 
  ABSTRACT  
 
The three-dimensional structure of hen egg-white lysozyme (HEWL) in a hexagonal crystal form has been determined and refined to 1.46 A resolution. This hexagonal crystal form crystallizes from a saturated sodium nitrate solution at pH 8.4. The crystals belong to space group P6(1)22, with unit-cell parameters a = b = 85.64, c = 67.93 A. A total of 165 water molecules, 16 nitrate ions and five sodium ions were located in the electron-density map. The hexagonal crystal form exhibits a higher solvent content and a higher degree of disorder than other crystal forms of lysozyme. The flexibility of the protein depends on the crystal packing, although some residue ranges are flexible in all native HEWL crystal forms.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 (a) and (b) Na132 and (c) and (d) Na133 in the hexagonal HEWL crystal form. The twofold symmetry axes are indicated. The distances between sodium and connected O atoms are shown in (b) and (d), respectively. (2F[o] - F[c]) maps contoured at 1.0 . Distances are given in Å. Figures were generated using MOLSCRIPT v2.1.2 (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]), BOBSCRIPT (Esnouf, 1997[Esnouf, R. M. (1997). J. Mol. Graph. 15, 132-134.]) and RASTER3D v2.7b (Merritt & Bacon, 1997[Merritt, E. A. & Bacon, D. J. (1997). Methods Enzymol. 277, 505-524.]).
Figure 3.
Figure 3 C^ superposition of HEWL crystal forms (triclinic, monoclinic, orthorhombic and tetragonal structures; Brinkmann et al., 2006[Brinkmann, C., Weiss, M. S. & Weckert, E. (2006). In preparation.]) and of HEWL, GEWL and TEWL. Calculations were performed using the program LSQKAB (Collaborative Computional Project, Number 4, 1994[Collaborative Computational Project, Number 4 (1994). Acta Cryst. D50, 760-763.]). Figures were generated using MOLSCRIPT v2.1.2 (Kraulis, 1991[Kraulis, P. J. (1991). J. Appl. Cryst. 24, 946-950.]).
 
  The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2006, 62, 349-355) copyright 2006.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19554207 A.L.Grzesiak, and A.J.Matzger (2008).
Selection of Protein Crystal Forms Facilitated by Polymer-Induced Heteronucleation.
  Cryst Growth Des, 8, 347-350.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.

 

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