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EBI PDBe PDBeView

PDBe Entry: 2oqx view

Crystal Structure of the apo form of E. coli tryptophanase at 1.9 A resolution
Summary
Header LYASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.9 Å, R-factor: 21.0%, Free R-factor: 23.2%, Spacegroup: F 2 2 2
Released 20/02/2007, deposition: 01/02/2007, last revision: 24/02/2009
Authors Goldgur, Y.search; Kogan, A.search; Gdalevsky, G.search; Parola, A.search; Cohen-Luria, R.search; Almog, O.search
Primary citation The structure of apo tryptophanase from Escherichia coli reveals a wide-open conformation.
ACTA CRYSTALLOGR.,SECT.Dsearch vol:63, pag:969-974 (2007) [PubMed ID 17704565 ]search
Keywords LYASEsearch, PYRIDOXAL PHOSPHATEsearch, TRYPTOPHAN CATABOLISMsearch
EC 4.1.99.1 ExPASy BRENDA search (A)
Organism Escherichia coli 562search(A)
UniProt Tryptophanase (EC 4.1.99.1) (L-tryptophan indole-lyase) (TNase) P0A853search (A)
Solvent A
Related entries 1ax4, 2c44, 1tpl
Polymers
Id Name Type UniProt Residues Observed
A Tryptophanase Protein P0A853 (TNAA_ECOLI)search
 467 99%
Heterogens
Id Name Ligands
A CHLORIDE ION CL search
A MAGNESIUM ION MG search
A 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID EPE search
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