Structure of PDB 2tsy Chain A

Receptor sequence
>2tsyA (length=262) [Search protein sequence]
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALEL
GVPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLL
MYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAP
IFICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENHHLIEKLKEYHAA
PALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELR
SFVSAMKAASRA
3D structure
PDB2tsy Crystal structures of a mutant (betaK87T) tryptophan synthase alpha2beta2 complex with ligands bound to the active sites of the alpha- and beta-subunits reveal ligand-induced conformational changes.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E49 D60 Y175
Catalytic site (residue number reindexed from 1) E49 D60 Y175
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 G3P A F22 Y175 T183 G184 F212 G213 G234 S235 F22 Y175 T183 G184 F206 G207 G228 S229
Gene Ontology
Molecular Function
GO:0004834 tryptophan synthase activity
GO:0005515 protein binding
GO:0016829 lyase activity
Biological Process
GO:0000162 tryptophan biosynthetic process
GO:0006568 tryptophan metabolic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2tsy, PDBe:2tsy, PDBj:2tsy
PDBsum2tsy
PubMed9201907
UniProtP00929|TRPA_SALTY Tryptophan synthase alpha chain (Gene Name=trpA)

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