› 4gsa

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE) REDUCED WITH CYANOBOROHYDRATE

Released:
DOI: 10.2210/pdb4gsa/pdb
PDB entry 4gsa coloured by chain, front view.
PDB entry 4gsa coloured by chain, side view.
PDB entry 4gsa coloured by chain, top view.
Source organism: Synechococcus sp.
Primary publication:
Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity.
Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN
Proc Natl Acad Sci U S A 94 4866-71 (1997)
PMID: 9144156

Function and Biology Details

Reaction catalysed: 
(S)-4-amino-5-oxopentanoate = 5-aminolevulinate
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-150263 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate-1-semialdehyde 2,1-aminomutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 432 amino acids
Theoretical weight: 46.06 KDa
Source organism: Synechococcus sp.
Expression system: Escherichia coli
UniProt:
  • Canonical: P24630 (Residues: 2-433; Coverage: 100%)
Gene names: gsa, hemL, syc0881_c
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


Cofactor: Ligand PLP 2 x PLP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P212121
Unit cell:
a: 68.64Å b: 108.28Å c: 122.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.187 0.264
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Pyridoxal phosphate enzymes: mechanistic, structural, and evolutionary considerations.
Eliot et al. (2004)
12 more

1 mention without citation

Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity.
Hennig et al. (1997)