› 2gsa

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF GLUTAMATE-1-SEMIALDEHYDE AMINOMUTASE (AMINOTRANSFERASE, WILD-TYPE FORM)

Released:
DOI: 10.2210/pdb2gsa/pdb
PDB entry 2gsa coloured by chain, front view.
PDB entry 2gsa coloured by chain, side view.
PDB entry 2gsa 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 1 x PLP

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ELLIOTT GX-21
Spacegroup: P212121
Unit cell:
a: 68.62Å b: 108.6Å c: 122.43Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.25
Expression system: Escherichia coli

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Citations

13 review citations

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

10 mentions 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)
9 more