› 1h7d

Solution NMR

Solution structure of the 49 aa presequence of 5-ALAS

Released:
DOI: 10.2210/pdb1h7d/pdb
PDB entry 1h7d coloured by chain, ensemble of 30 models, front view.
PDB entry 1h7d coloured by chain, ensemble of 30 models, side view.
PDB entry 1h7d coloured by chain, ensemble of 30 models, top view.
Source organism: Mus musculus
Primary publication:
The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase.
Goodfellow BJ, Dias JS, Ferreira GC, Henklein P, Wray V, Macedo AL
FEBS Lett 505 325-31 (2001)
PMID: 11566198

Function and Biology Details

Reaction catalysed: 
Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140288 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5-aminolevulinate synthase, erythroid-specific, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 49 amino acids
Theoretical weight: 5.1 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P08680 (Residues: 1-49; Coverage: 8%)
Gene name: Alas2
Sequence domains: 5-aminolevulinate synthase presequence
Structure domains: Aminolevulinic Acid Synthase 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Not provided

Quick links

Citations

3 review citations

Mechanisms of mitochondrial dysfunction and energy deficiency in Alzheimer's disease.
Atamna et al. (2007)
2 more

1 mention without citation

Fold-recognition and comparative modeling of human alpha2,3-sialyltransferases reveal their sequence and structural similarities to CstII from Campylobacter jejuni.
Sujatha et al. (2006)