Structure of PDB 2dh5 Chain A

Receptor sequence
>2dh5A (length=393) Species: 562 (Escherichia coli) [Search protein sequence]
TLLNPYFGEFGGMYVPQILMPALRQLEEAFVSAQKDPEFQAQFNDLLKNY
AGRPTALTKCQNITAGTNTTLYLKREDLLHGGAHKTNQVLGQALLAKRMG
KTEIIAETGAGQHGVASALASALLGLKCRIYMGAKDVERQSPNVFRMRLM
GAEVIPVHSGSATLKDACNEALRDWSGSYETAHYMLGTAAGPHPYPTIVR
EFQRMIGEETKAQILEREGRLPDAVIACVGGGSNAIGMFADFINETNVGL
IGVEPGGHGIETGEHGAPLKHGRVGIYFGMKAPMMQTEQIEESYSISAGL
DFPSVGPQHAYLNSTGRADYVSITDDEALEAFKTLCLHEGIIPALESSHA
LAHALKMMRENPDKEQLLVVNLSGRGDKDIFTVHDILKARGEI
3D structure
PDB2dh5 Large conformational changes in the Escherichia coli tryptophan synthase beta(2) subunit upon pyridoxal 5'-phosphate binding
ChainA
Resolution2.9 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 S373
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 A H86 K87 T190 G232 G234 S235 N236 E350 S377 G378 H84 K85 T188 G230 G232 S233 N234 E346 S373 G374
Gene Ontology
Molecular Function
GO:0004834 tryptophan synthase activity
GO:0016829 lyase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0006568 tryptophan metabolic process
GO:0009073 aromatic amino acid family biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2dh5, PDBe:2dh5, PDBj:2dh5
PDBsum2dh5
PubMed20370823
UniProtP0A879|TRPB_ECOLI Tryptophan synthase beta chain (Gene Name=trpB)

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