Brand  (β version)

PDB ID: 1K8Y

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Ligands
Code Name Style Show Link
13P 1,3-dihydroxyacetonephosphate PoSSuM
NA Sodium ion PoSSuM
PLP Pyridoxal-5'-phosphate PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1K8Y   PDBj   RCSB PDB   PDBe
Header : LYASE
Title : CRYSTAL STRUCTURE OF THE TRYPTOPHAN SYNTHASE BETA-SER178PRO MUTANT COMPLEXED WITH D,L-ALPHA-GLYCEROL-3-PHOSPHATE
Release Data : 2002-06-19
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: S178P
Source :
mol_id organism_scientific expression_system
1 Salmonella typhimurium  (taxid:602) Escherichia coli  (taxid:562)
gene: TRPA/TRPB
expression_system_strain: CB149
expression_system_vector_type: PLASMID
expression_system_plasmid: PSTB7
mol_id organism_scientific expression_system
2 Salmonella typhimurium  (taxid:602) Escherichia coli  (taxid:562)
gene: TRPA/TRPB
expression_system_strain: CB149
expression_system_vector_type: PLASMID
expression_system_plasmid: PSTB7
Authors : Weyand, M., Schlichting, I., Marabotti, A., Mozzarelli, A.
Keywords : CARBON-OXYGEN LYASE, TRYPTOPHAN BIOSYNTHESIS, PYRIDOXAL PHOSPHATE, LYASE
Exp. method : X-RAY DIFFRACTION ( 1.50 Å )
Citation :

Crystal structure of the beta Ser178--> Pro mutant of tryptophan synthase. A "knock-out" allosteric enzyme.

Weyand, M.,Schlichting, I.,Herde, P.  et al.
(2002)  J.Biol.Chem.  277 : 10653 - 10660

PubMed: 11756454
DOI: 10.1074/jbc.M111031200

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 - -