Structure of PDB 3nl6 Chain C

Receptor sequence
>3nl6C (length=513) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence]
FSKEQFDYSLYLVTDSGMIPEGKTLYGQVEAGLQNGVTLVQIREKDADTK
FFIEEALQIKELCHAHNVPLIINDRIDVAMAIGADGIHVGQDDMPIPMIR
KLVGPDMVIGWSVGFPEEVDELSKMGPDMVDYIGVGTLPTLTMGTAGAIR
VLDALERNNAHWCRTVGIGGLHPDNIERVLYQCVSSNGKRSLDGICVVSD
IIASLDAAKSTKILRGLIDKTDYKFVNIGLSTKNSLTTTDEIQSIISNTL
KARPLVQHITNKVHQNFGANVTLALGSSPIMSEIQSEVNDLAAIPHATLL
LNTGSVAPPEMLKAAIRAYNDVKRPIVFDPVGYSATETRLLLNNKLLTFG
QFSCIKGNSSEILGLAELSNELLIQATKIVAFKYKTVAVCTGEFDFIADG
TIEGKYSLSTNGTSVEDIPCVAVEAGPIEIMGDITASGCSLGSTIACMIG
GQPSEGNLFHAVVAGVMLYKAAGKIASEKCNGSGSFQVELIDALYRLTRE
NTPVTWAPKLTHT
3D structure
PDB3nl6 Domain Organization in Candida glabrata THI6, a Bifunctional Enzyme Required for Thiamin Biosynthesis in Eukaryotes .
ChainC
Resolution2.612 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
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.
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 C Q43 R45 H90 S114 T139 T143 T145 I179 G181 S210 Q41 R43 H88 S112 T137 T140 T142 I168 G170 S199
BS02 ACP C N369 T416 G417 E418 D420 G453 I455 M458 A463 G465 K497 N358 T391 G392 E393 D395 G426 I428 M431 A436 G438 K470
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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