Structure of PDB 2tsy Chain A Binding Site BS01
Receptor Information
>2tsy Chain A (length=262) [
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MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALEL
GVPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLL
MYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAP
IFICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENHHLIEKLKEYHAA
PALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELR
SFVSAMKAASRA
Ligand information
Ligand ID
G3P
InChI
InChI=1S/C3H9O6P/c4-1-3(5)2-9-10(6,7)8/h3-5H,1-2H2,(H2,6,7,8)/t3-/m1/s1
InChIKey
AWUCVROLDVIAJX-GSVOUGTGSA-N
SMILES
Software
SMILES
OpenEye OEToolkits 1.7.6
C(C(COP(=O)(O)O)O)O
CACTVS 3.385
OC[C@@H](O)CO[P](O)(O)=O
ACDLabs 12.01
O=P(OCC(O)CO)(O)O
OpenEye OEToolkits 1.7.6
C([C@H](COP(=O)(O)O)O)O
CACTVS 3.385
OC[CH](O)CO[P](O)(O)=O
Formula
C3 H9 O6 P
Name
SN-GLYCEROL-3-PHOSPHATE
ChEMBL
CHEMBL1232920
DrugBank
DB02515
ZINC
ZINC000003830896
PDB chain
2tsy Chain A Residue 271 [
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Receptor-Ligand Complex Structure
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PDB
2tsy
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.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
F22 Y175 T183 G184 F212 G213 G234 S235
Binding residue
(residue number reindexed from 1)
F22 Y175 T183 G184 F206 G207 G228 S229
Annotation score
2
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.
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
View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2tsy
,
PDBe:2tsy
,
PDBj:2tsy
PDBsum
2tsy
PubMed
9201907
UniProt
P00929
|TRPA_SALTY Tryptophan synthase alpha chain (Gene Name=trpA)
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