Structure of PDB 1a50 Chain B

Receptor sequence
>1a50B (length=390) [Search protein sequence]
TTLLNPYFGEFGGMYVPQILMPALNQLEEAFVRAQKDPEFQAQFADLLKN
YAGRPTALTKCQNITAGTRTTLYLKREDLLHGGAHKTNQVLGQALLAKRM
GKSEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRL
MGAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIV
REFQRMIGEETKAQILDKEGRLPDAVIACVGGGSNAIGMFADFINDTSVG
LIGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTADGQIEESYSIS
AGLDFPSVGPQHAYLNSIGRADYVSITDDEALEAFKTLCRHEGIIPALES
SHALAHALKMMREQPEKEQLLVVNLSGRGDKDIFTVHDIL
3D structure
PDB1a50 Loop closure and intersubunit communication in tryptophan synthase.
ChainB
Resolution2.3 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 T110 T190 G232 G233 G234 S235 N236 S351 S377
Catalytic site (residue number reindexed from 1) K86 E108 T109 T189 G231 G232 G233 S234 N235 S350 S376
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 G233 G234 S235 N236 E350 S377 G378 H85 K86 T189 G231 G232 G233 S234 N235 E349 S376 G377
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:1a50, PDBe:1a50, PDBj:1a50
PDBsum1a50
PubMed9548921
UniProtP0A2K1|TRPB_SALTY Tryptophan synthase beta chain (Gene Name=trpB)

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