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The structure of D-mandelate dehydrogenase with L103G and T143G mutations

X-ray diffraction
2.55Å resolution
PDB entry 8wl4 coloured by chain, front view.
PDB entry 8wl4 coloured by chain, side view.
PDB entry 8wl4 coloured by chain, top view.
Source organism: Levilactobacillus brevis
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: 2-dehydropantoate 2-reductase
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Multimeric state: homo dimer
Accessible surface area: 26069.63 Å2
Buried surface area: 1948.57 Å2
Dissociation area: 974.29 Å2
Dissociation energy (ΔGdiss): 8.59 kcal/mol
Dissociation entropy (TΔSdiss): 13.39 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-285561

Macromolecules

2-dehydropantoate 2-reductase
Chains: A, B
Length: 312 amino acids
Theoretical weight: 33.28 KDa
Source organism: Levilactobacillus brevis
Expression system: Escherichia coli BL21(DE3)
2-dehydropantoate 2-reductase in PDB entry 8wl4, assembly 1, front view.
2-dehydropantoate 2-reductase in PDB entry 8wl4, assembly 1, side view.
2-dehydropantoate 2-reductase in PDB entry 8wl4, assembly 1, top view.
131220406080100120140160180200220240260280300
 
100200300
Chains
Chain A (auth A)
Chain B (auth B)
Sequence conservation
Molecule details ›

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