› 1xym

X-ray diffraction
1.8Å resolution

THE ROLE OF THE DIVALENT METAL ION IN SUGAR BINDING, RING OPENING, AND ISOMERIZATION BY D-XYLOSE ISOMERASE: REPLACEMENT OF A CATALYTIC METAL BY AN AMINO-ACID

Released:
DOI: 10.2210/pdb1xym/pdb
PDB entry 1xym coloured by chain, front view.
PDB entry 1xym coloured by chain, side view.
PDB entry 1xym coloured by chain, top view.
Source organism: Streptomyces olivochromogenes
Primary publication:
Role of the divalent metal ion in sugar binding, ring opening, and isomerization by D-xylose isomerase: replacement of a catalytic metal by an amino acid.
Allen KN, Lavie A, Glasfeld A, Tanada TN, Gerrity DP, Carlson SC, Farber GK, Petsko GA, Ringe D
Biochemistry 33 1488-94 (1994)
PMID: 7906142

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-147411 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xylose isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 386 amino acids
Theoretical weight: 42.84 KDa
Source organism: Streptomyces olivochromogenes
Expression system: Not provided
UniProt:
  • Canonical: P15587 (Residues: 2-387; Coverage: 100%)
Gene name: xylA
Sequence domains: Xylose isomerase-like TIM barrel
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

3 bound ligands:
Ligand GLO 2 x GLO
Ligand MG 2 x MG
Ligand OH 2 x OH
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21212
Unit cell:
a: 88.12Å b: 99.53Å c: 94.79Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 not available
Expression system: Not provided

Quick links

Citations

3 review citations

Quantum mechanical methods for enzyme kinetics.
Gao et al. (2002)
2 more

1 mention without citation

From the similarity analysis of protein cavities to the functional classification of protein families using cavbase.
Kuhn et al. (2006)