3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.99.1
BRENDA Enzyme Link: BRENDA 4.1.99.1
KEGG Enzyme Link: KEGG4.1.99.1
BioCyc Enzyme Link: BioCyc 4.1.99.1
ExPASy Enzyme Link: ExPASy4.1.99.1
EC2PDB Enzyme Link: EC2PDB 4.1.99.1
ExplorEnz Enzyme Link: ExplorEnz 4.1.99.1
PRIAM enzyme-specific profiles Link: PRIAM 4.1.99.1
IntEnz Enzyme Link: IntEnz 4.1.99.1
MEDLINE Enzyme Link: MEDLINE 4.1.99.1
MSA:

4.1.99.1;

Phylogenetic Tree:

4.1.99.1;

Uniprot:
M-CSA:
RHEA:19553 H2O + L-tryptophan = indole + NH4(+) + pyruvate
RULE(radius=1) [*:1]:[c;H0;+0:2](:[*:3])-[CH2;+0:4]-[CH;+0:5](-[*:6])-[NH2;+0:7].[OH2;+0:8]>>[*:6]-[C;H0;+0:5](-[CH3;+0:4])=[O;H0;+0:8].[*:1]:[cH;+0:2]:[*:3].[NH3;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Crystal structure of tryptophanase.Isupov MN, Antson AA, Dodson EJ, Dodson GG, Dementieva IS, Zakomirdina LN, Wilson KS, Dauter Z, Lebedev AA, Harutyunyan EH1998 Feb 279551100
Tryptophanase: structure, catalytic activities, and mechanism of action.Snell EE1975236639
Structure of Escherichia coli tryptophanase.Ku SY, Yip P, Howell PL2006 Jul16790938