› 1t4z

Solution NMR

Solution structure of the N-terminal domain of Synechococcus elongatus SasA (25-structures ensemble)

Released:
DOI: 10.2210/pdb1t4z/pdb
PDB entry 1t4z coloured by chain, ensemble of 25 models, front view.
PDB entry 1t4z coloured by chain, ensemble of 25 models, side view.
PDB entry 1t4z coloured by chain, ensemble of 25 models, top view.
Source organism: Synechococcus elongatus PCC 7942 = FACHB-805
Primary publication:
Structure of the N-terminal domain of the circadian clock-associated histidine kinase SasA.
Vakonakis I, Klewer DA, Williams SB, Golden SS, LiWang AC
J Mol Biol 342 9-17 (2004)
PMID: 15313603

Function and Biology Details

Reaction catalysed: 
ATP + protein L-histidine = ADP + protein N-phospho-L-histidine
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170411 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adaptive-response sensory kinase SasA Chain: A
Molecule details ›
Chain: A
Length: 105 amino acids
Theoretical weight: 11.48 KDa
Source organism: Synechococcus elongatus PCC 7942 = FACHB-805
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q06904 (Residues: 4-103; Coverage: 26%)
Gene names: Synpcc7942_2114, sarS, sasA
Sequence domains: KaiB domain
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing, slow refinement in the presence of database potentials
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Circadian Rhythms in Cyanobacteria.
Cohen et al. (2015)
9 more

1 mention without citation

Predicting continuous local structure and the effect of its substitution for secondary structure in fragment-free protein structure prediction.
Faraggi et al. (2009)