Structure of PDB 1tjp Chain A Binding Site BS01

Receptor Information
>1tjp Chain A (length=267) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALEL
GVPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLL
MYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAP
IFICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENRGALPLHHLIEKL
KEYHAAPALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQ
MLAELRSFVSAMKAASR
Ligand information
Ligand IDHPF
InChIInChI=1S/C9H14NO7P/c11-7-4-2-1-3-6(7)10-9(13)8(12)5-17-18(14,15)16/h1-4,8-13H,5H2,(H2,14,15,16)/t8-,9-/m1/s1
InChIKeySPOVITMZOKMJPQ-RKDXNWHRSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc(c(c1)N[C@@H]([C@@H](COP(=O)(O)O)O)O)O
ACDLabs 10.04O=P(O)(O)OCC(O)C(O)Nc1ccccc1O
CACTVS 3.341O[C@H](CO[P](O)(O)=O)[C@@H](O)Nc1ccccc1O
OpenEye OEToolkits 1.5.0c1ccc(c(c1)NC(C(COP(=O)(O)O)O)O)O
CACTVS 3.341O[CH](CO[P](O)(O)=O)[CH](O)Nc1ccccc1O
FormulaC9 H14 N O7 P
Name1-[(2-HYDROXYLPHENYL)AMINO]3-GLYCEROLPHOSPHATE
ChEMBL
DrugBank
ZINCZINC000033913600
PDB chain1tjp Chain A Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1tjp On the structural basis of the catalytic mechanism and the regulation of the alpha subunit of tryptophan synthase from Salmonella typhimurium and BX1 from maize, two evolutionarily related enzymes.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		E49 D60 I64 L100 Y175 T183 G184 F212 G213 G234 S235
Binding residue
(residue number reindexed from 1)		E49 D60 I64 L100 Y175 T183 G184 F212 G213 G234 S235
Annotation score2
Binding affinityPDBbind-CN: -logKd/Ki=4.42,Kd=38uM
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:1tjp, PDBe:1tjp, PDBj:1tjp
PDBsum1tjp
PubMed16120446
UniProtP00929|TRPA_SALTY Tryptophan synthase alpha chain (Gene Name=trpA)

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