Structure of PDB 3nl3 Chain F

Receptor sequence
>3nl3F (length=502) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence]
KFSKEQFDYSLYLVTDSGMIPEGKTLYGQVEAGLQNGVLVQIRADTKFFI
EEALQIKELCHAHNVPLIINDRIDVAMAIGADGIHVGQDDMPIPMIRKLV
GPDMVIGWSVGFPEEVDELSKMGPDMVDYIGVGTLFPTLTKGTAGAIRVL
DALERNNAHWCRTVGIGGLHPDNIERVLYQCVSSNGKRSLDGICVVSDII
ASLDAAKSTKILRGLIDKTDYKFVNIGLSTKNSLTTTDEIQSIISNTLKA
RPLVQHITNKVHQNFGANVTLALGSSPIMSEIQSEVNDLAAIPHATLLLN
TGSVAPPEMLKAAIRAYNDVKRPIVFDPVGYSATETRLLLNNKLLTFGQF
SCIKGNSSEILGLAELSNELLIQATKIVAFKYKTVAVCTGEFDFIADGTI
EGKYSLSKGTTSVEDIPCVAVEAGPIGCSLGSTIACMIGGQPSEGNLFHA
VVAGVMLYKAAGKIASEKCNGSGSFQVELIDALYRLTRENTPVTWAPKLT
HT
3D structure
PDB3nl3 Domain Organization in Candida glabrata THI6, a Bifunctional Enzyme Required for Thiamin Biosynthesis in Eukaryotes .
ChainF
Resolution3.007 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R45 S114 K146
Catalytic site (residue number reindexed from 1) R43 S109 K141
Enzyme Commision number 2.5.1.3: thiamine phosphate synthase.
2.7.1.50: hydroxyethylthiazole kinase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 TPS F Q43 H90 S114 T143 T145 I179 G181 V209 S210 Q41 H85 S109 T138 T140 I166 G168 V196 S197
BS02 MG F P341 E372 P328 E359
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:3nl3, PDBe:3nl3, PDBj:3nl3
PDBsum3nl3
PubMed20968298
UniProtQ6FV03

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