› 1jeo

X-ray diffraction
2Å resolution

Crystal Structure of the Hypothetical Protein MJ1247 from Methanococcus jannaschii at 2.0 A Resolution Infers a Molecular Function of 3-Hexulose-6-Phosphate isomerase.

Released:
DOI: 10.2210/pdb1jeo/pdb
PDB entry 1jeo coloured by chain, front view.
PDB entry 1jeo coloured by chain, side view.
PDB entry 1jeo coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A resolution infers a molecular function of 3-hexulose-6-phosphate isomerase.
Martinez-Cruz LA, Dreyer MK, Boisvert DC, Yokota H, Martinez-Chantar ML, Kim R, Kim SH
Structure 10 195-204 (2002)
PMID: 11839305

Function and Biology Details

Reaction catalysed: 
D-arabino-hex-3-ulose 6-phosphate = D-fructose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-176668 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-hexulose-6-phosphate isomerase Chain: A
Molecule details ›
Chain: A
Length: 180 amino acids
Theoretical weight: 20.7 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q58644 (Residues: 1-180; Coverage: 100%)
Gene names: MJ1247, phi
Sequence domains: SIS domain
Structure domains: Glucose-6-phosphate isomerase like protein; domain 1

Ligands and Environments

1 bound ligand:
Ligand CIT 1 x CIT
1 modified residue:
Ligand CME 3 x CME

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: I222
Unit cell:
a: 67.921Å b: 68.155Å c: 83.336Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.189 0.226
Expression system: Escherichia coli BL21(DE3)

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Citations

5 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
4 more

6 mentions without citation

On the role of aggregation prone regions in protein evolution, stability, and enzymatic catalysis: insights from diverse analyses.
Buck et al. (2013)
5 more