› 1w3u

X-ray diffraction
1.5Å resolution

Crystal structure of phosphoserine aminotransferase from Bacillus circulans var. alkalophilus

Released:
DOI: 10.2210/pdb1w3u/pdb
PDB entry 1w3u coloured by chain, front view.
PDB entry 1w3u coloured by chain, side view.
PDB entry 1w3u coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus.
Dubnovitsky AP, Kapetaniou EG, Papageorgiou AC
Protein Sci 14 97-110 (2005)
PMID: 15608117

Function and Biology Details

Reaction catalysed: 
4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176780 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoserine aminotransferase Chain: A
Molecule details ›
Chain: A
Length: 362 amino acids
Theoretical weight: 39.97 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59196 (Residues: 1-362; Coverage: 100%)
Gene name: serC
Sequence domains: Aminotransferase class-V
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 1 x PLP
1 bound ligand:
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: C2
Unit cell:
a: 91.287Å b: 91.109Å c: 42.374Å
α: 90° β: 111.25° γ: 90°
R-values:
R R work R free
0.144 not available 0.208
Expression system: Escherichia coli

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Citations

4 review citations

Alkaline pH homeostasis in bacteria: new insights.
Padan et al. (2005)
3 more

1 mention without citation

Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus.
Dubnovitsky et al. (2005)