› 1mb4

X-ray diffraction
1.84Å resolution

Crystal structure of aspartate semialdehyde dehydrogenase from vibrio cholerae with NADP and S-methyl-l-cysteine sulfoxide

Released:
DOI: 10.2210/pdb1mb4/pdb
PDB entry 1mb4 coloured by chain, front view.
PDB entry 1mb4 coloured by chain, side view.
PDB entry 1mb4 coloured by chain, top view.
Source organism: Vibrio cholerae
Primary publication:
A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae.
Blanco J, Moore RA, Kabaleeswaran V, Viola RE
Protein Sci 12 27-33 (2003)
PMID: 12493825

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 domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192028 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate-semialdehyde dehydrogenase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 370 amino acids
Theoretical weight: 40.54 KDa
Source organism: Vibrio cholerae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KQG2 (Residues: 1-370; Coverage: 100%)
Gene names: VC_2036, asd1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 2 x NDP
1 bound ligand:
Ligand CYS 2 x CYS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P43212
Unit cell:
a: 107.63Å b: 107.63Å c: 153.538Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.192 0.229
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Bacterial methionine biosynthesis.
Ferla et al. (2014)
1 more

3 mentions without citation

A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae.
Blanco et al. (2003)
2 more