4ot8

X-ray diffraction
2Å resolution

X-ray Crystal Structure of Serine Hydroxymethyl Transferase from Burkholderia cenocepacia bound to PLP and Serine

Released:
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-110023 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine hydroxymethyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 423 amino acids
Theoretical weight: 45.98 KDa
Source organism: Burkholderia cenocepacia J2315
Expression system: Escherichia coli
UniProt:
  • Canonical: B4ECY9 (Residues: 1-415; Coverage: 100%)
Gene names: BCAL3197, glyA
Sequence domains: Serine hydroxymethyltransferase
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 4 x PLP
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 66.22Å b: 179.84Å c: 75.64Å
α: 90° β: 115.25° γ: 90°
R-values:
R R work R free
0.168 0.165 0.206
Expression system: Escherichia coli