› 2uyt

X-ray diffraction
1.55Å resolution

Structure of L-rhamnulose kinase in complex with ADP and beta-L- rhamnulose.

Released:
DOI: 10.2210/pdb2uyt/pdb
PDB entry 2uyt coloured by chain, front view.
PDB entry 2uyt coloured by chain, side view.
PDB entry 2uyt coloured by chain, top view.
Source organism: Escherichia coli BL21(DE3)
Primary publication:
Substrate spectrum of L-rhamnulose kinase related to models derived from two ternary complex structures.
Grueninger D, Schulz GE
FEBS Lett 581 3127-30 (2007)
PMID: 17568582

Function and Biology Details

Reaction catalysed: 
ATP + L-rhamnulose = ADP + L-rhamnulose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173035 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhamnulokinase Chain: A
Molecule details ›
Chain: A
Length: 489 amino acids
Theoretical weight: 53.95 KDa
Source organism: Escherichia coli BL21(DE3)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q1R415 (Residues: 1-489; Coverage: 100%)
Gene names: UTI89_C4487, rhaB
Sequence domains:
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

2 bound ligands:
Ligand LRH 1 x LRH
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 51.043Å b: 51.093Å c: 158.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.209
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Regulation of the rhaEWRBMA Operon Involved in l-Rhamnose Catabolism through Two Transcriptional Factors, RhaR and CcpA, in Bacillus subtilis.
Hirooka et al. (2015)
3 more

1 mention without citation

The FGGY carbohydrate kinase family: insights into the evolution of functional specificities.
Zhang et al. (2011)