3mkn

X-ray diffraction
2Å resolution

Crystal structure of the E. coli pyrimidine nucleosidase YeiK bound to a competitive inhibitor

Released:

Function and Biology Details

Reaction catalysed:
A pyrimidine nucleoside + H(2)O = D-ribose + a pyrimidine base
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pyrimidine-specific ribonucleoside hydrolase RihB Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 316 amino acids
Theoretical weight: 34.04 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: C3T3U2 (Residues: 1-313; Coverage: 100%)
Gene names: ECs3054, EXX13_03090, TUM18780_15040, rihB
Sequence domains: Inosine-uridine preferring nucleoside hydrolase
Structure domains: Ribonucleoside hydrolase-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21
Unit cell:
a: 84.851Å b: 86.446Å c: 97.817Å
α: 90° β: 98.86° γ: 90°
R-values:
R R work R free
0.175 0.174 0.196
Expression system: Escherichia coli BL21(DE3)