Structure of PDB 2wsy Chain B

Receptor sequence
>2wsyB (length=375) [Search protein sequence]
TLLNPYFGEFGGMYVPQILMPALNQLEEAFVRAQKDPEFQAQFADLLKNY
AGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRMG
KSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDSPNVFRMRLMGAEV
ITLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVREFQRMIGEETK
AQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVGLIGVEPGGHGIE
TGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSISAGLDFPSVGPQH
AYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALESSHALAHALKMMR
EQPEKEQLLVVNLSGRGDKDIFTVH
3D structure
PDB2wsy Loop closure and intersubunit communication in tryptophan synthase.
ChainB
Resolution3.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K87 E109 S377
Catalytic site (residue number reindexed from 1) K85 E107 S364
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 PLP B H86 K87 T190 G232 G234 S235 N236 L304 E350 S377 G378 H84 K85 T177 G219 G221 S222 N223 L291 E337 S364 G365
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:2wsy, PDBe:2wsy, PDBj:2wsy
PDBsum2wsy
PubMed9548921
UniProtP0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)

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