› 1nc5

X-ray diffraction
1.6Å resolution

Structure of Protein of Unknown Function of YteR from Bacillus Subtilis

Released:
DOI: 10.2210/pdb1nc5/pdb
PDB entry 1nc5 coloured by chain, front view.
PDB entry 1nc5 coloured by chain, side view.
PDB entry 1nc5 coloured by chain, top view.
Source organism: Bacillus subtilis
Primary publication:
1.6 A crystal structure of YteR protein from Bacillus subtilis, a predicted lyase.
Zhang R, Minh T, Lezondra L, Korolev S, Moy SF, Collart F, Joachimiak A
Proteins 60 561-5 (2005)
PMID: 15906318

Function and Biology Details

Reaction catalysed: 
2-O-(4-deoxy-beta-L-threo-hex-4-enopyranuronosyl)-alpha-L-rhamnopyranose + H(2)O = 5-dehydro-4-deoxy-D-glucuronate + L-rhamnopyranose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Unsaturated rhamnogalacturonyl hydrolase YteR Chain: A
Molecule details ›
Chain: A
Length: 373 amino acids
Theoretical weight: 43.02 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
UniProt:
  • Canonical: O34559 (Residues: 1-373; Coverage: 100%)
Gene names: BSU30120, yteR
Sequence domains: Glycosyl Hydrolase Family 88
Structure domains: Glycosyltransferase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6122
Unit cell:
a: 91.855Å b: 91.855Å c: 179.41Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.187 0.187 0.214
Expression system: Escherichia coli

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Citations

3 citation in other articles

A novel glycoside hydrolase family 105: the structure of family 105 unsaturated rhamnogalacturonyl hydrolase complexed with a disaccharide in comparison with family 88 enzyme complexed with the disaccharide.
Itoh et al. (2006)
2 more

5 mentions without citation

Identification of the ligand binding sites on the molecular surface of proteins.
Kinoshita et al. (2005)
4 more