› 2xtb

X-ray diffraction
2.8Å resolution

Crystal Structure of Trypanosoma brucei rhodesiense Adenosine Kinase Complexed with Activator

Released:
DOI: 10.2210/pdb2xtb/pdb
Model geometry
Fit model/data
PDB entry 2xtb coloured by chain, front view.
PDB entry 2xtb coloured by chain, side view.
PDB entry 2xtb coloured by chain, top view.
Source organism: Trypanosoma brucei rhodesiense
Primary publication:
Crystal structures of T. b. rhodesiense adenosine kinase complexed with inhibitor and activator: implications for catalysis and hyperactivation.
Kuettel S, Greenwald J, Kostrewa D, Ahmed S, Scapozza L, Perozzo R
OpenAccess logo PLoS Negl Trop Dis 5 e1164 (2011)
PMID: 21629723

Function and Biology Details

Reaction catalysed: 
ATP + adenosine = ADP + AMP
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosine kinase Chain: A
Molecule details ›
Chain: A
Length: 347 amino acids
Theoretical weight: 38.13 KDa
Source organism: Trypanosoma brucei rhodesiense
Expression system: Escherichia coli
UniProt:
  • Canonical: Q584S0 (Residues: 1-345; Coverage: 100%)
Gene names: Tb06.4M18.780, Tb927.6.2360
Sequence domains: pfkB family carbohydrate kinase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand KRM 1 x KRM
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P41212
Unit cell:
a: 61.24Å b: 61.24Å c: 193.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.232 0.296
Expression system: Escherichia coli

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Citations

2 review citations

Adenosine kinase: exploitation for therapeutic gain.
Boison D. (2013)
1 more

4 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
3 more