Structure of PDB 3nl6 Chain A Binding Site BS01

Receptor Information
>3nl6 Chain A (length=518) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KFSKEQFDYSLYLVTSGMIPEGKTLYGQVEAGLQNGVTLVQIREKDADTK
FFIEEALQIKELCHAHNVPLIINDRIDVAMAIGADGIHVGQDDMPIPMIR
KLVGPDMVIGWSVGFPEEVDELSKMGPVDYIGVGTLFPTLTKKAPMGTAG
AIRVLDALERNNAHWCRTVGIGGLHPDNIERVLYQCVSSNGKRSLDGICV
VSDIIASLDAAKSTKILRGLIDKTDYKFVNIGLSTKNSLTTTDEIQSIIS
NTLKARPLVQHITNKVHQNFGANVTLALGSSPIMSEIQSEVNDLAAIPHA
TLLLNTGSVAPPEMLKAAIRAYNDVKRPIVFDPVGYSATETRLLLNNKLL
TFGQFSCIKGNSSEILGLAELSNELLIQATKIVAFKYKTVAVCTGEFDFI
ADGTIEGKYSLSKGTNGTSVEDIPCVAVEAGPIEIMGDITASGCSLGSTI
ACMIGGQPSEGNLFHAVVAGVMLYKAAGKIASEKCNGSGSFQVELIDALY
RLTRENTPVTWAPKLTHT
Ligand information
Ligand IDTPS
InChIInChI=1S/C12H17N4O4PS/c1-8-11(3-4-20-21(17,18)19)22-7-16(8)6-10-5-14-9(2)15-12(10)13/h5,7H,3-4,6H2,1-2H3,(H3-,13,14,15,17,18,19)/p+1
InChIKeyHZSAJDVWZRBGIF-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(C[n+]2csc(CCO[P](O)(O)=O)c2C)c(N)n1
OpenEye OEToolkits 1.5.0Cc1c(sc[n+]1Cc2cnc(nc2N)C)CCOP(=O)(O)O
ACDLabs 10.04O=P(O)(O)OCCc1sc[n+](c1C)Cc2c(nc(nc2)C)N
FormulaC12 H18 N4 O4 P S
NameTHIAMIN PHOSPHATE
ChEMBLCHEMBL1236378
DrugBank
ZINCZINC000001532839
PDB chain3nl6 Chain A Residue 2001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3nl6 Domain Organization in Candida glabrata THI6, a Bifunctional Enzyme Required for Thiamin Biosynthesis in Eukaryotes .
Resolution2.612 Å
Binding residue
(original residue number in PDB)		Q43 R45 H90 S114 T139 T143 T145 I179 V209 S210
Binding residue
(residue number reindexed from 1)		Q41 R43 H88 S112 T135 T139 T141 I171 V201 S202
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) R45 S114
Catalytic site (residue number reindexed from 1) R43 S112
Enzyme Commision number 2.5.1.3: thiamine phosphate synthase.
2.7.1.50: hydroxyethylthiazole kinase.
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004417 hydroxyethylthiazole kinase activity
GO:0004789 thiamine-phosphate diphosphorylase activity
GO:0005524 ATP binding
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0009228 thiamine biosynthetic process
GO:0009229 thiamine diphosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3nl6, PDBe:3nl6, PDBj:3nl6
PDBsum3nl6
PubMed20968298
UniProtQ6FV03

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