Structure of PDB 1kfb Chain A Binding Site BS01

Receptor Information
>1kfb Chain A (length=255) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MERYENLFAQLNDRREGAFVPFVTLGDPGIEQSLKIIDTLIDAGADALEL
GVPFSDPLADGPTIQNANLRAFAAGVTPAQCFEMLALIREKHPTIPIGLL
MYANLVFNNGIDAFYARCEQVGVDSVLVADVPVEESAPFRQAALRHNIAP
IFICPPNADDDLLRQVASYGRGYTYLLSRLHHLIEKLKEYHAAPALQGFG
ISSPEQVSAAVRAGAAGAISGSAIVKIIEKNLASPKQMLAELRSFVSAMK
AASRA
Ligand information
Ligand IDIGP
InChIInChI=1S/C11H14NO6P/c13-10(6-18-19(15,16)17)11(14)8-5-12-9-4-2-1-3-7(8)9/h1-5,10-14H,6H2,(H2,15,16,17)/t10-,11+/m1/s1
InChIKeyNQEQTYPJSIEPHW-MNOVXSKESA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc2c(c1)c(c[nH]2)C(C(COP(=O)(O)O)O)O
CACTVS 3.341O[CH](CO[P](O)(O)=O)[CH](O)c1c[nH]c2ccccc12
OpenEye OEToolkits 1.5.0c1ccc2c(c1)c(c[nH]2)[C@@H]([C@@H](COP(=O)(O)O)O)O
CACTVS 3.341O[C@H](CO[P](O)(O)=O)[C@@H](O)c1c[nH]c2ccccc12
ACDLabs 10.04O=P(O)(O)OCC(O)C(O)c2c1ccccc1nc2
FormulaC11 H14 N O6 P
NameINDOLE-3-GLYCEROL PHOSPHATE
ChEMBL
DrugBankDB04143
ZINC
PDB chain1kfb Chain A Residue 550 [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]
PDB1kfb On the Role of alphaTHR183 in the Allosteric Regulation and Catalytic Mechanism of Tryptophan Synthase
Resolution1.9 Å
Binding residue
(original residue number in PDB)		F22 D60 L100 A129 Y175 F212 G213 G234 S235
Binding residue
(residue number reindexed from 1)		F22 D60 L100 A129 Y175 F199 G200 G221 S222
Annotation score5
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:1kfb, PDBe:1kfb, PDBj:1kfb
PDBsum1kfb
PubMed12460570
UniProtP00929|TRPA_SALTY Tryptophan synthase alpha chain (Gene Name=trpA)

[Back to BioLiP]