Structure of PDB 1g67 Chain A

Receptor sequence
>1g67A (length=225) Species: 1423 (Bacillus subtilis) [Search protein sequence]
GIRMTRISREMMKELLSVYFIMGSNNTKADPVTVVQKALKGGATLYQFRE
KGGDALTGEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIHIGQ
EDANAKEVRAAIGDMILGVAAHTMSEVKQAEEDGADYVGLGPIYPTETKK
DTRAVQGVSLIEAVRRQGISIPIVGIGGITIDNAAPVIQAGADGVSMISA
ISQAEDPESAARKFREEIQTYKTGR
3D structure
PDB1g67 Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase.
ChainA
Resolution1.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R59 A130 K159
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 A D93 D112 D83 D102
BS02 ICP A Y29 Q57 H107 I186 Y19 Q47 H97 I176
BS03 POP A R59 K61 D93 G109 A130 K159 R49 K51 D83 G99 A120 K149
BS04 TZP A R59 T156 T158 K159 I186 G188 M207 I208 S209 R49 T146 T148 K149 I176 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

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Cellular Component
External links
PDB RCSB:1g67, PDBe:1g67, PDBj:1g67
PDBsum1g67
PubMed11513589
UniProtP39594|THIE_BACSU Thiamine-phosphate synthase (Gene Name=thiE)

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