› 2glk

X-ray diffraction
0.94Å resolution

High-resolution study of D-Xylose isomerase, 0.94A resolution.

Released:
DOI: 10.2210/pdb2glk/pdb
PDB entry 2glk coloured by chain, front view.
PDB entry 2glk coloured by chain, side view.
PDB entry 2glk coloured by chain, top view.
Source organism: Streptomyces rubiginosus
Primary publication:
Locating active-site hydrogen atoms in D-xylose isomerase: time-of-flight neutron diffraction.
Katz AK, Li X, Carrell HL, Hanson BL, Langan P, Coates L, Schoenborn BP, Glusker JP, Bunick GJ
Proc Natl Acad Sci U S A 103 8342-7 (2006)
PMID: 16707576

Function and Biology Details

Reaction catalysed: 
Alpha-D-xylopyranose = alpha-D-xylufuranose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150204 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xylose isomerase Chain: A
Molecule details ›
Chain: A
Length: 388 amino acids
Theoretical weight: 43.28 KDa
Source organism: Streptomyces rubiginosus
UniProt:
  • Canonical: P24300 (Residues: 1-388; Coverage: 100%)
Gene name: xylA
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

2 bound ligands:
Ligand MN 2 x MN
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: I222
Unit cell:
a: 92.712Å b: 97.935Å c: 101.867Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.116 0.115 0.128

Quick links

Citations

4 review citations

Industrial use of immobilized enzymes.
DiCosimo et al. (2013)
3 more

6 mentions without citation

Accurate SAXS profile computation and its assessment by contrast variation experiments.
Schneidman-Duhovny et al. (2013)
5 more