Function and Biology Details
Reaction catalysed:
(1a) 1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Tryptophan synthase, alpha chain
- Tryptophan synthase beta chain-like, PALP domain superfamily
- Tryptophan synthase beta chain/beta chain-like
- Tryptophan synthase, beta chain
- Tryptophan synthase, beta chain, conserved site
- Tryptophan synthase beta chain-like, PALP domain
- Tryptophan synthase, alpha chain, active site
- Ribulose-phosphate binding barrel
1 more domain
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Tryptophan synthase (preferred)
PDBe Complex ID:
PDB-CPX-186373 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tryptophan synthase alpha chain
Molecule details ›
Chains: A, C, E, G, I, K
Length: 248 amino acids
Theoretical weight: 27.54 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I
Length: 248 amino acids
Theoretical weight: 27.54 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8U094 (Residues: 1-248; Coverage: 100%)
Sequence domains: Tryptophan synthase alpha chain
Structure domains: Aldolase class I
Tryptophan synthase beta chain 1
Molecule details ›
Chains: B, D, F, H, J, L
Length: 385 amino acids
Theoretical weight: 42.32 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold
Length: 385 amino acids
Theoretical weight: 42.32 KDa
Source organism: Pyrococcus furiosus
Expression system: Escherichia coli
UniProt:
- Canonical: Q8U093 (Residues: 1-385; Coverage: 99%)
Sequence domains: Pyridoxal-phosphate dependent enzyme
Structure domains: Rossmann fold
