› 2hta

X-ray diffraction
1.9Å resolution

Crystal Structure of a putative mutarotase (YeaD) from Salmonella typhimurium in orthorhombic form

Released:
DOI: 10.2210/pdb2hta/pdb
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PDB entry 2hta coloured by chain, front view.
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PDB entry 2hta coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Primary publication:
Structure of the putative mutarotase YeaD from Salmonella typhimurium: structural comparison with galactose mutarotases.
Chittori S, Simanshu DK, Savithri HS, Murthy MR
Acta Crystallogr D Biol Crystallogr 63 197-205 (2007)
PMID: 17242513

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-187346 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative glucose-6-phosphate 1-epimerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 34.34 KDa
Source organism: Salmonella enterica subsp. enterica serovar Typhimurium
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8ZPV9 (Residues: 1-294; Coverage: 100%)
Gene names: STM1289, yeaD
Sequence domains: Aldose 1-epimerase
Structure domains: Beta-galactosidase; Chain A, domain 5

Ligands and Environments

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

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P212121
Unit cell:
a: 49.751Å b: 88.774Å c: 179.294Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.223
Expression system: Escherichia coli

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Citations

1 citations in other articles

Multiplex PCR using YeaD and 16S rRNA gene to identify major pathogens in vibriosis of Litopenaeus vannamei.
Han et al. (2019)

3 mentions without citation

Structure-based function analysis of putative conserved proteins with isomerase activity from Haemophilus influenzae.
Shahbaaz et al. (2015)
2 more

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