Brand  (β version)

PDB ID: 2J9Y

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Ligands
Code Name Style Show Link
FOO (3e)-4-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}-2-iminobut-3-enoic acid PoSSuM
NA Sodium ion PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 2J9Y   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : Tryptophan Synthase Q114N mutant in complex with Compound II
Release Data : 2007-12-04
Compound :
mol_id molecule chains
1 TRYPTOPHAN SYNTHASE ALPHA CHAIN A
ec: 4.2.1.20
mol_id molecule chains
2 TRYPTOPHAN SYNTHASE BETA CHAIN B
ec: 4.2.1.20
mutation: YES
Source :
mol_id organism_scientific expression_system
1 SALMONELLA TYPHIMURIUM  (taxid:602) ESCHERICHIA COLI  (taxid:562)
expression_system_strain: CB149
expression_system_plasmid: PSTB7
mol_id organism_scientific expression_system
2 SALMONELLA TYPHIMURIUM  (taxid:602) ESCHERICHIA COLI  (taxid:562)
expression_system_vector: PSTB7
Authors : Blumenstein, L., Domratcheva, T., Niks, D., Ngo, H., Seidel, R., Dunn, M.F., Schlichting, I.
Keywords : AROMATIC AMINO ACID BIOSYNTHESIS, TRYPTOPHAN BIOSYNTHESIS, LYASE CARBON- OXYGEN LYASE, AMINO-ACID BIOSYNTHESIS, LYASE, ALLOSTERIC ENZYME, PYRIDOXAL PHOSPHATE
Exp. method : X-RAY DIFFRACTION ( 1.80 Å )
Citation :

Betaq114N and Betat110V Mutations Reveal a Critically Important Role of the Substrate Alpha-Carboxylate Site in the Reaction Specificity of Tryptophan Synthase.

Blumenstein, L.,Domratcheva, T.,Niks, D.  et al.
(2007)  Biochemistry  46 : 14100

PubMed: 18004874
DOI: 10.1021/BI7008568

Reaction

Chain : A
UniProt : P00929 (TRPA_SALTY)
Reaction: EC: Evidence:
Physiological Direction:
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D- glyceraldehyde 3-phosphate + L-tryptophan + H2O 4.2.1.20 HAMAP-Rule:MF_00131
-
Chain : B
UniProt : P0A2K1 (TRPB_SALTY)
Reaction: EC: Evidence:
Physiological Direction:
(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D- glyceraldehyde 3-phosphate + L-tryptophan + H2O 4.2.1.20 -
-
Cofactor: Evidence: Note:
pyridoxal 5'-phosphate - -