› 1e5q

X-ray diffraction
2.1Å resolution

Ternary complex of saccharopine reductase from Magnaporthe grisea, NADPH and saccharopine

Released:
DOI: 10.2210/pdb1e5q/pdb
PDB entry 1e5q coloured by chain, front view.
PDB entry 1e5q coloured by chain, side view.
PDB entry 1e5q coloured by chain, top view.
Source organism: Pyricularia grisea
Primary publication:
Crystal structure of saccharopine reductase from Magnaporthe grisea, an enzyme of the alpha-aminoadipate pathway of lysine biosynthesis.
Johansson E, Steffens JJ, Lindqvist Y, Schneider G
Structure 8 1037-47 (2000)
PMID: 11080625

Function and Biology Details

Reaction catalysed: 
N(6)-(L-1,3-dicarboxypropyl)-L-lysine + NADP(+) + H(2)O = L-glutamate + (S)-2-amino-6-oxohexanoate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192853 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Saccharopine dehydrogenase [NADP(+), L-glutamate-forming] Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 450 amino acids
Theoretical weight: 49.16 KDa
Source organism: Pyricularia grisea
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9P4R4 (Residues: 1-450; Coverage: 100%)
Gene names: LYS3, MGG_08564
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NDP 8 x NDP
1 bound ligand:
Ligand SHR 8 x SHR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P21
Unit cell:
a: 86.643Å b: 205.809Å c: 125.599Å
α: 90° β: 100.05° γ: 90°
R-values:
R R work R free
0.207 0.207 0.228
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The enzymes of oxalate metabolism: unexpected structures and mechanisms.
Svedruzić et al. (2005)
2 more

7 mentions without citation

Evolution and multifarious horizontal transfer of an alternative biosynthetic pathway for the alternative polyamine sym-homospermidine.
Shaw et al. (2010)
6 more