Structure of PDB 3o15 Chain A

Receptor sequence

>3o15A (length=219) Species: 1423 (Bacillus subtilis)

TRISREMMKELLSVYFIMGSNNTKADPVTVVQKALKGGATLYQFREKGGD
ALTGEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIHIGQEDAN
AKEVRAAIGDMILGVSAHTMSEVKQAEEDGADYVGLGPIYPTETKKDTRA
VQGVSLIEAVRRQGISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQA
EDPESAARKFREEIQTYKT

3D structure

• PDB: 3o15 Crystal Structure and Kinetic Characterization of Bacillus subtilis Thiamin Phosphate Synthase with a Carboxylated Thiazole Phosphate
• Chain: A
• Resolution: 1.95 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R59 S130 K159
• Catalytic site (residue number reindexed from 1): R45 S116 K145
• Enzyme Commision number: 2.5.1.3: thiamine phosphate synthase.

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	3NM	A	R59 G151 P152 T156 T158 K159 T162 I186 G188 M207 I208 S209	R45 G137 P138 T142 T144 K145 T148 I172 G174 M193 I194 S195
BS02	IFP	A	Y29 Q57 H107 S130 V184 I186 S206	Y15 Q43 H93 S116 V170 I172 S192
BS03	POP	A	R59 K61 D93 G109 S130 K159	R45 K47 D79 G95 S116 K145

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004789 thiamine-phosphate diphosphorylase activity
• 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

External links

• PDB: RCSB:3o15, PDBe:3o15, PDBj:3o15
• PDBsum: 3o15
• UniProt: P39594|THIE_BACSU Thiamine-phosphate synthase (Gene Name=thiE)