Structure of PDB 3nm1 Chain E Binding Site BS04

Receptor Information
>3nm1 Chain E (length=505) Species: 5478 (Nakaseomyces glabratus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KFSKEQFDYSLYLVTDSGMIPEGKTLYGQVEAGNGVTLVQIREKDADTKF
FIEEALQIKELCHAHNVPLIINDRIDVAMAIGADGIHVGQDDMPIPMIRK
LVGMVIGWSVGFPEEVDELSKMGPVDYIGVGTLFPTLTKKNPKKAPMGTA
GAIRVLDALERNNAHWCRTVGIGGLHPDNIERVLYQCVSSNGKRSLDGIC
VVSDIIASLDAAKSTKILRGLIDKTDYKFVNIGLSSLTTTDEIQSIISNT
LKARPLVQHITNKVHQNFGANVTLALGSSPIMSEIQSEVNDLAAIPHATL
LLNTGSVAPPEMLKAAIRAYNDVKRPIVFDPVGYSATETRLLLNNLLLTF
GQFSCIKGNSSEILGLAELSNELLIQATKIVAFKYKTVAVCTGEFDFIAD
GTIEGKYSLSTNGTSVEDIPCVAVEAGPIGCSLGSTIACMIGGQPSEGNL
FHAVVAGVMLYKAAGKIASEKCNGSGSFQVELIDALYRLTRENTPVTWAP
KLTHT
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3nm1 Chain E Residue 544 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3nm1 Domain Organization in Candida glabrata THI6, a Bifunctional Enzyme Required for Thiamin Biosynthesis in Eukaryotes .
Resolution3.211 Å
Binding residue
(original residue number in PDB)		D76 D95
Binding residue
(residue number reindexed from 1)		D73 D92
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) R45 S114 K146
Catalytic site (residue number reindexed from 1) R42 S109 K139
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3nm1, PDBe:3nm1, PDBj:3nm1
PDBsum3nm1
PubMed20968298
UniProtQ6FV03

[Back to BioLiP]