Structure of PDB 1beu Chain B

Receptor sequence
>1beuB (length=389) [Search protein sequence]
TLLNPYFGEFGGMYVPQILMPALNQLEEAFVRAQKDPEFQAQFADLLKNY
AGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMG
KSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLM
GAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVR
EFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVGL
IGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISA
GLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALESS
HALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDIL
3D structure
PDB1beu Cryocrystallography and microspectrophotometry of a mutant (alpha D60N) tryptophan synthase alpha 2 beta 2 complex reveals allosteric roles of alpha Asp60.
ChainB
Resolution1.9 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 4.2.1.20: tryptophan synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PLS B H86 K87 T110 G111 A112 Q114 H115 T190 G232 G234 S235 N236 A302 G303 E350 S377 H84 K85 T108 G109 A110 Q112 H113 T188 G230 G232 S233 N234 A300 G301 E348 S375
Gene Ontology
Molecular Function
GO:0004834 tryptophan synthase activity
GO:0005515 protein binding
GO:0016829 lyase activity
GO:0042802 identical protein binding
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0006568 tryptophan metabolic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1beu, PDBe:1beu, PDBj:1beu
PDBsum1beu
PubMed9692955
UniProtP0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)

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