Structure of PDB 1g6c Chain A

Receptor sequence
>1g6cA (length=226) Species: 1423 (Bacillus subtilis) [Search protein sequence]
HGIRMTRISREMMKELLSVYFIMGSNNTKADPVTVVQKALKGGATLYQFR
EKGGDALTGEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIHIG
QEDANAKEVRAAIGDMILGVAAHTMSEVKQAEEDGADYVGLGPIYPTETK
KDTRAVQGVSLIEAVRRQGISIPIVGIGGITIDNAAPVIQAGADGVSMIS
AISQAEDPESAARKFREEIQTYKTGR
3D structure
PDB1g6c 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) R50 A121 K150
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 D84 D103
BS02 IFP A Y29 I31 Q57 H107 Y147 I186 S206 Y20 I22 Q48 H98 Y138 I177 S197
BS03 POP A R59 K61 N92 D93 G109 K159 R50 K52 N83 D84 G100 K150
BS04 TZP A R59 T156 T158 K159 G188 M207 I208 S209 R50 T147 T149 K150 G179 M198 I199 S200
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1g6c, PDBe:1g6c, PDBj:1g6c
PDBsum1g6c
PubMed11513589
UniProtP39594|THIE_BACSU Thiamine-phosphate synthase (Gene Name=thiE)

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