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PDBsum entry 4zbc

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protein ligands metals Protein-protein interface(s) links
Isomerase PDB id
4zbc

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
387 a.a.
Ligands
GLC ×2
FRU ×4
GLC-GLC
Metals
_MN ×11
Waters ×542
PDB id:
4zbc
Name: Isomerase
Title: A dehydrated form of glucose isomerase collected at 100k.
Structure: Xylose isomerase. Chain: a, b. Synonym: glucose isomerase. Engineered: yes
Source: Streptomyces rubiginosus. Organism_taxid: 1929. Gene: xyla. Expressed in: streptomyces rubiginosus. Expression_system_taxid: 1929
Resolution:
2.00Å     R-factor:   0.138     R-free:   0.182
Authors: J.Sandy
Key ref: C.M.Lobley et al. (2016). A generic protocol for protein crystal dehydration using the HC1b humidity controller. Acta Crystallogr D Struct Biol, 72, 629-640. PubMed id: 27139626 DOI: 10.1107/S2059798316003065
Date:
14-Apr-15     Release date:   23-Mar-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P24300  (XYLA_STRRU) -  Xylose isomerase from Streptomyces rubiginosus
Seq:
Struc:
388 a.a.
387 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.5.3.1.5  - xylose isomerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: alpha-D-xylose = alpha-D-xylulofuranose
alpha-D-xylose
Bound ligand (Het Group name = GLC)
matches with 83.33% similarity
= alpha-D-xylulofuranose
      Cofactor: Mg(2+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Key reference    
 
 
DOI no: 10.1107/S2059798316003065 Acta Crystallogr D Struct Biol 72:629-640 (2016)
PubMed id: 27139626  
 
 
A generic protocol for protein crystal dehydration using the HC1b humidity controller.
C.M.Lobley, J.Sandy, J.Sanchez-Weatherby, M.Mazzorana, T.Krojer, R.P.Nowak, T.L.Sorensen.
 
  ABSTRACT  
 
Dehydration may change the crystal lattice and affect the mosaicity, resolution and quality of X-ray diffraction data. A dehydrating environment can be generated around a crystal in several ways with various degrees of precision and complexity. This study uses a high-precision crystal humidifier/dehumidifier to provide an airstream of known relative humidity in which the crystals are mounted: a precise yet hassle-free approach to altering crystal hydration. A protocol is introduced to assess the impact of crystal dehydration systematically applied to nine experimental crystal systems. In one case, that of glucose isomerase, dehydration triggering a change of space group from I222 to P21212 was observed. This observation is supported by an extended study of the behaviour of the glucose isomerase crystal structure during crystal dehydration.
 

 

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