› 2cfb

X-ray diffraction
2.85Å resolution

Glutamate-1-semialdehyde 2,1-Aminomutase from Thermosynechococcus elongatus

Released:
DOI: 10.2210/pdb2cfb/pdb
PDB entry 2cfb coloured by chain, front view.
PDB entry 2cfb coloured by chain, side view.
PDB entry 2cfb coloured by chain, top view.
Source organism: Synechococcus elongatus
Primary publication:
Evolutionary relationship between initial enzymes of tetrapyrrole biosynthesis.
Schulze JO, Schubert WD, Moser J, Jahn D, Heinz DW
J Mol Biol 358 1212-20 (2006)
PMID: 16564539

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-184105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate-1-semialdehyde 2,1-aminomutase Chain: A
Molecule details ›
Chain: A
Length: 411 amino acids
Theoretical weight: 43.55 KDa
Source organism: Synechococcus elongatus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8DLK8 (Residues: 27-437; Coverage: 94%)
Gene names: hemL, tlr0479
Sequence domains: Aminotransferase class-III
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P41212
Unit cell:
a: 108.92Å b: 108.92Å c: 93.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.173 0.22
Expression system: Escherichia coli BL21

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Citations

12 review citations

Tetrapyrrole biosynthesis in higher plants.
Tanaka et al. (2007)
11 more