3l44

X-ray diffraction
2.05Å resolution

Crystal structure of Bacillus anthracis HemL-1, glutamate semialdehyde aminotransferase

Released:
Entry authors: Anderson SM, Wawrzak Z, Gordon E, Hasseman J, Edwards A, Savchenko A, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate-1-semialdehyde 2,1-aminomutase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 434 amino acids
Theoretical weight: 47.24 KDa
Source organism: Bacillus anthracis str. 'Ames Ancestor'
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q81YV0 (Residues: 1-434; Coverage: 100%)
Gene names: BAS0499, BA_0531, GBAA_0531, hemL1
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments

No bound ligands
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 75.84Å b: 93.92Å c: 105.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.157 0.192
Expression system: Escherichia coli BL21(DE3)