Structure of PDB 3nm3 Chain A

Receptor sequence

>3nm3A (length=510) Species: 5478 (Nakaseomyces glabratus)

KFSKEQFDYSLYLVTDSGMIPEGKTLYGQVEAGLQNGVTLVQIREKDADT
KFFIEEALQIKELCHAHNVPLIINDRIDVAMAIGADGIHVGQDDMPIPMI
RKLVGPDMVIGWSVGFPEEVDELSKMGPDMVDYIGVGTLFPTLTKKNPMG
TAGAIRVLDALERNNAHWCRTVGIGGLHPDNIERVLYQCVSSNGKRSLDG
ICVVSDIIASLDAAKSTKILRGLIDKTDYKFVNIGLSTKNSLTTTDEIQS
IISNTLKARPLVQHITNKVHQNFGANVTLALGSSPIMSEIQSEVNDLAAI
PHATLLLNTGSVAPPEMLKAAIRAYNDVKRPIVFDPVGATETRLLLNNKL
LTFGQFSCIKGNSSEILGLAELSNELLIQATKIVAFKYKTVAVCTGEFDF
IADGTIEGKYSLSKGTNGTSVEDIPCVAVEAGPIGCSLGSTIACMIGGQP
SEGNLFHAVVAGVMLYKAAGKIASEKCNGSGSFQVELIDALYRLTRENTP
VTWAPKLTHT

3D structure

• PDB: 3nm3 Domain Organization in Candida glabrata THI6, a Bifunctional Enzyme Required for Thiamin Biosynthesis in Eukaryotes .
• Chain: A
• Resolution: 3.102 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	MG	A	D76 D95	D75 D94
BS02	TPS	A	Q43 R45 H90 S114 T143 T145 I179 G181 V209 S210	Q42 R44 H89 S113 T142 T144 I174 G176 V204 S205
BS03	POP	A	R45 K47 N75 G92 S114 K146	R44 K46 N74 G91 S113 K145

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:3nm3, PDBe:3nm3, PDBj:3nm3
• PDBsum: 3nm3
• PubMed: 20968298
• UniProt: Q6FV03