› 3fa3

X-ray diffraction
2.6Å resolution

Crystal structure of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member, trigonal crystal form

Released:
DOI: 10.2210/pdb3fa3/pdb
PDB entry 3fa3 coloured by chain, front view.
PDB entry 3fa3 coloured by chain, side view.
PDB entry 3fa3 coloured by chain, top view.
Source organism: Aspergillus niger
Primary publication:
Structure and function of 2,3-dimethylmalate lyase, a PEP mutase/isocitrate lyase superfamily member.
Narayanan B, Niu W, Joosten HJ, Li Z, Kuipers RK, Schaap PJ, Dunaway-Mariano D, Herzberg O
J Mol Biol 386 486-503 (2009)
PMID: 19133276

Function and Biology Details

Reaction catalysed: 
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = pyruvate + succinate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173700 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxaloacetate hydrolase class protein Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P
Length: 302 amino acids
Theoretical weight: 32.02 KDa
Source organism: Aspergillus niger
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2L887 (Residues: 2-303; Coverage: 100%)
Gene names: An07g08390, AnigIFM63604_010932, CAN33_0017865
Sequence domains: Phosphoenolpyruvate phosphomutase
Structure domains: Phosphoenolpyruvate-binding domains

Ligands and Environments

3 bound ligands:
Ligand MN 16 x MN
Ligand OAF 14 x OAF
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P32
Unit cell:
a: 160.57Å b: 160.57Å c: 161.41Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.19 0.255
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

3DM: systematic analysis of heterogeneous superfamily data to discover protein functionalities.
Kuipers et al. (2010)
8 more

1 mention without citation

Structure of oxalacetate acetylhydrolase, a virulence factor of the chestnut blight fungus.
Chen et al. (2010)