› 1smk

X-ray diffraction
2.5Å resolution

Mature and translocatable forms of glyoxysomal malate dehydrogenase have different activities and stabilities but similar crystal structures

Released:
DOI: 10.2210/pdb1smk/pdb
PDB entry 1smk coloured by chain, front view.
PDB entry 1smk coloured by chain, side view.
PDB entry 1smk coloured by chain, top view.
Source organism: Citrullus lanatus
Primary publication:
Organelle and translocatable forms of glyoxysomal malate dehydrogenase. The effect of the N-terminal presequence.
Cox B, Chit MM, Weaver T, Gietl C, Bailey J, Bell E, Banaszak L
FEBS J 272 643-54 (2005)
PMID: 15670147

Function and Biology Details

Reaction catalysed: 
(S)-malate + NAD(+) = oxaloacetate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148580 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Malate dehydrogenase, glyoxysomal Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 326 amino acids
Theoretical weight: 34.44 KDa
Source organism: Citrullus lanatus
Expression system: Escherichia coli
UniProt:
  • Canonical: P19446 (Residues: 37-356; Coverage: 90%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 137.43Å b: 88.05Å c: 138.819Å
α: 90° β: 91.53° γ: 90°
R-values:
R R work R free
0.207 0.204 0.254
Expression system: Escherichia coli

Quick links

Citations

11 citation in other articles

Dual specificities of the glyoxysomal/peroxisomal processing protease Deg15 in higher plants.
Helm et al. (2007)
10 more

2 mentions without citation

Predicting the accuracy of protein-ligand docking on homology models.
Bordogna et al. (2011)
1 more