Function and Biology Details
Reactions catalysed:
(1a) L-serine = 2-aminoprop-2-enoate + H(2)O
(1a) L-threonine = 2-aminobut-2-enoate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
L-serine dehydratase/L-threonine deaminase (preferred)
PDBe Complex ID:
PDB-CPX-148854 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-serine dehydratase/L-threonine deaminase
Molecule details ›
Chain: A
Length: 372 amino acids
Theoretical weight: 39.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold
Length: 372 amino acids
Theoretical weight: 39.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P20132 (Residues: 1-328; Coverage: 100%)
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold
