Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
F6R Fructose -6-phosphate
GOL Glycerol
SO4 Sulfate ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 1X9H   PDBj   RCSB PDB   PDBe
Header : ISOMERASE
Title : Crystal structure of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum in complex with fructose 6-phosphate
Release Data : 2004-12-07
Compound :
mol_id molecule chains
1 glucose-6-phosphate isomerase A,B
ec: 5.3.1.9, 5.3.1.8
Source :
mol_id organism_scientific expression_system
1 Pyrobaculum aerophilum  (taxid:13773) Escherichia coli  (taxid:562)
gene: PAE1610
expression_system_strain: JM109
expression_system_vector_type: plasmid
expression_system_plasmid: pET17b
Authors : Swan, M.K., Hansen, T., Schoenheit, P., Davies, C.
Keywords : enzyme, crenarchaeon, hyperthermophile, PGI superfamily, fructose 6-phosphate, ISOMERASE
Exp. method : X-RAY DIFFRACTION ( 1.50 Å )
Citation :

Structural basis for phosphomannose isomerase activity in phosphoglucose isomerase from Pyrobaculum aerophilum: a subtle difference between distantly related enzymes.

Swan, M.K.,Hansen, T.,Schoenheit, P.  et al.
(2004)  Biochemistry  43 : 14088 - 14095

PubMed: 15518558
DOI: 10.1021/bi048608y

A novel phosphoglucose isomerase/phosphomannose isomerase from the crenarchaeon Pyrobaculum aerophilum is a member of the PGI superfamily: structural evidence at 1.16 A resolution

Swan, M.K.,Hansen, T.,Schoenheit, P.  et al.
To be published 

Crystallization and preliminary X-ray diffraction analysis of phosphoglucose/phosphomannose isomerase from Pyrobaculum aerophilum

Swan, M.K.,Hansen, T.,Schoenheit, P.  et al.
(2004)  Acta Crystallogr.,Sect.D  60 : 1481 - 1483