Structure of PDB 3nl3 Chain D

Receptor sequence

>3nl3D (length=504) Species: 5478 (Nakaseomyces glabratus)

KFSKEQFDYSLYLVTDSGMIPEGKTLYGQVEAGLQNGVTLVQIREKDADT
KFFIEEALQIKELCHAHNVPLIINDRIDVAMAIGADGIHVGQDDMPIPMI
RKLVGPDMVIGWSVGFPEEVDELSKMGPDMVDYIGVGTLFPTLTKKNPGT
AGAIRVLDALERNNAHWCRTVGIGGLHPDNIERVLYQCVSSNGKRSLDGI
CVVSDIIASLDAAKSTKILRGLIDKTDYKFVNIGLSTKNSLTTTDEIQSI
ISNTLKARPLVQHITNKVHQNFGANVTLALGSSPIMSEIQSEVNDLAAIP
HATLLLNTGSVAPPEMLKAAIRAYNDVKRPIVFDPVGYSATETRLLLNNK
LLTFGQFSCIKGNSSEILGLAELSNELLIQATKIVAFKYKTVAVCTGEFD
FIADGTIEGKYSLSKGTNTSVEDIPCVAVESLGSTIACMIGGQPSEGNLF
HAVVAGVMLYKAAGKIASEKCNGSGSFQVELIDALYRLTRENTPVTWAPK
LTHT

3D structure

• PDB: 3nl3 Domain Organization in Candida glabrata THI6, a Bifunctional Enzyme Required for Thiamin Biosynthesis in Eukaryotes .
• Chain: D
• Resolution: 3.007 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R45 S114 K146
• Catalytic site (residue number reindexed from 1): R44 S113 K145
• 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	D	Q43 R45 H90 S114 T143 T145 I179 G181 V209 S210	Q42 R44 H89 S113 T142 T144 I173 G175 V203 S204
BS02	MG	D	A49 T51	A48 T50
BS03	MG	D	P341 E372	P335 E366

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

External links

• PDB: RCSB:3nl3, PDBe:3nl3, PDBj:3nl3
• PDBsum: 3nl3
• PubMed: 20968298
• UniProt: Q6FV03