X-ray diffraction
1.4Å resolution

Crystal structure of Glutamate-1-semialdehyde 2,1-aminomutase from Stenotrophomonas maltophilia K279a in complex with PLP

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

Function and Biology Details

Reaction catalysed:
(S)-4-amino-5-oxopentanoate = 5-aminolevulinate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Glutamate-1-semialdehyde 2,1-aminomutase Chain: A
Molecule details ›
Chain: A
Length: 437 amino acids
Theoretical weight: 46.14 KDa
Source organism: Stenotrophomonas maltophilia K279a
Expression system: Escherichia coli BL21(DE3)
  • Canonical: B2FT35 (Residues: 1-429; Coverage: 100%)
Gene names: Smlt3873, hemL
Sequence domains: Aminotransferase class-III

Ligands and Environments

Cofactor: Ligand PLP 1 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P6522
Unit cell:
a: 60.28Å b: 60.28Å c: 367.22Å
α: 90° β: 90° γ: 120°
R R work R free
0.136 0.134 0.181
Expression system: Escherichia coli BL21(DE3)