Structure of PDB 1fuy Chain A Binding Site BS01

Receptor Information
>1fuy Chain A (length=262) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALEL
GVPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLL
MYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAP
IFICPPNADDDLLRQVASYGRGYTYLLSRSGVTGAENLHHLIEKLKEYHA
APALQGFGISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAEL
RSFVSAMKAASR
Ligand information
Ligand IDFIP
InChIInChI=1S/C11H13FNO4P/c12-9-3-4-11-10(6-9)8(7-13-11)2-1-5-17-18(14,15)16/h3-4,6-7,13H,1-2,5H2,(H2,14,15,16)
InChIKeyYVYGGBFCYXRNKM-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1cc2c(cc1F)c(c[nH]2)CCCOP(=O)(O)O
CACTVS 3.341O[P](O)(=O)OCCCc1c[nH]c2ccc(F)cc12
ACDLabs 10.04Fc1cc2c(cc1)ncc2CCCOP(=O)(O)O
FormulaC11 H13 F N O4 P
Name5-FLUOROINDOLE PROPANOL PHOSPHATE
ChEMBLCHEMBL1160523
DrugBankDB07773
ZINCZINC000003606158
PDB chain1fuy Chain A Residue 269 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1fuy Structural basis for the impaired channeling and allosteric inter-subunit communication in the beta A169L/beta C170W mutant of tryptophan synthase.
Resolution2.25 Å
Binding residue
(original residue number in PDB)		F22 D60 Y175 T183 G184 F212 G213 S235
Binding residue
(residue number reindexed from 1)		F22 D60 Y175 T183 G184 F207 G208 S230
Annotation score1
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1fuy, PDBe:1fuy, PDBj:1fuy
PDBsum1fuy
PubMed11034989
UniProtP00929|TRPA_SALTY Tryptophan synthase alpha chain (Gene Name=trpA)

[Back to BioLiP]