Structure of PDB 1g67 Chain B

Receptor sequence

>1g67B (length=225) Species: 1423 (Bacillus subtilis)

GIRMTRISREMMKELLSVYFIMGSNNTKADPVTVVQKALKGGATLYQFRE
KGGDALTGEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIHIGQ
EDANAKEVRAAIGDMILGVAAHTMSEVKQAEEDGADYVGLGPIYPTETKK
DTRAVQGVSLIEAVRRQGISIPIVGIGGITIDNAAPVIQAGADGVSMISA
ISQAEDPESAARKFREEIQTYKTGR

3D structure

• PDB: 1g67 Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase.
• Chain: B
• Resolution: 1.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R1059 A1130 K1159
• Catalytic site (residue number reindexed from 1): R49 A120 K149
• 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	MG	B	D1093 D1112	D83 D102
BS02	ICP	B	Y1029 Q1057 H1107 I1186	Y19 Q47 H97 I176
BS03	POP	B	R1059 K1061 N1092 D1093 G1109 A1130 K1159	R49 K51 N82 D83 G99 A120 K149
BS04	TZP	B	R1059 T1156 T1158 K1159 G1188 M1207 I1208 S1209	R49 T146 T148 K149 G178 M197 I198 S199

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:1g67, PDBe:1g67, PDBj:1g67
• PDBsum: 1g67
• PubMed: 11513589
• UniProt: P39594|THIE_BACSU Thiamine-phosphate synthase (Gene Name=thiE)