› 1ys4

X-ray diffraction
2.29Å resolution

Structure of Aspartate-Semialdehyde Dehydrogenase from Methanococcus jannaschii

Released:
DOI: 10.2210/pdb1ys4/pdb
PDB entry 1ys4 coloured by chain, front view.
PDB entry 1ys4 coloured by chain, side view.
PDB entry 1ys4 coloured by chain, top view.
Source organism: Methanocaldococcus jannaschii
Primary publication:
A new branch in the family: structure of aspartate-beta-semialdehyde dehydrogenase from Methanococcus jannaschii.
Faehnle CR, Ohren JF, Viola RE
J Mol Biol 353 1055-68 (2005)
PMID: 16225889

Function and Biology Details

Reaction catalysed: 
L-aspartate 4-semialdehyde + phosphate + NADP(+) = L-4-aspartyl phosphate + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-176450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate-semialdehyde dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 354 amino acids
Theoretical weight: 39.96 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q57658 (Residues: 1-354; Coverage: 100%)
Gene names: MJ0205, asd
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 2 x NAP
1 bound ligand:
Ligand MLA 4 x MLA
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P43212
Unit cell:
a: 95.254Å b: 95.254Å c: 297.957Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.221
Expression system: Escherichia coli

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Citations

20 citation in other articles

Malonyl-coenzyme A reductase in the modified 3-hydroxypropionate cycle for autotrophic carbon fixation in archaeal Metallosphaera and Sulfolobus spp.
Alber et al. (2006)
19 more

4 mentions without citation

Structural basis for a bispecific NADP+ and CoA binding site in an archaeal malonyl-coenzyme A reductase.
Demmer et al. (2013)
3 more