› 2ciq

X-ray diffraction
1.7Å resolution

Structure-based functional annotation: Yeast ymr099c codes for a D- hexose-6-phosphate mutarotase.

Released:
DOI: 10.2210/pdb2ciq/pdb
PDB entry 2ciq coloured by chain, front view.
PDB entry 2ciq coloured by chain, side view.
PDB entry 2ciq coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structure-based functional annotation: yeast ymr099c codes for a D-hexose-6-phosphate mutarotase.
Graille M, Baltaze JP, Leulliot N, Liger D, Quevillon-Cheruel S, van Tilbeurgh H
J Biol Chem 281 30175-85 (2006)
PMID: 16857670

Function and Biology Details

Reaction catalysed: 
Alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169854 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucose-6-phosphate 1-epimerase Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 34 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q03161 (Residues: 1-297; Coverage: 100%)
Gene names: YM6543.06C, YMR099C
Sequence domains: Aldose 1-epimerase
Structure domains: Beta-galactosidase; Chain A, domain 5

Ligands and Environments

4 bound ligands:
Ligand EPE 1 x EPE
Ligand NA 1 x NA
Ligand GOL 1 x GOL
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 106.19Å b: 44.8Å c: 73.99Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.187 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

14 citation in other articles

MM-align: a quick algorithm for aligning multiple-chain protein complex structures using iterative dynamic programming.
Mukherjee et al. (2009)
13 more

1 mention without citation

Structure of the first representative of Pfam family PF09410 (DUF2006) reveals a structural signature of the calycin superfamily that suggests a role in lipid metabolism.
Chiu et al. (2010)