Structure of PDB 1g4p Chain B

Receptor sequence
>1g4pB (length=218) Species: 1423 (Bacillus subtilis) [Search protein sequence]
HGIRMTRISREMMKELLSVYFIMGSNNTKADPVTVVQKALKGGATLYQFR
EKGGDALTGEARIKFAEKAQAACREAGVPFIVNDDVELALNLKADGIHIG
QEDANAKEVRAAIGDMILGVAAHTMSEVKQAEEDGADYVGLGPIYPRAVQ
GVSLIEAVRRQGISIPIVGIGGITIDNAAPVIQAGADGVSMISAISQAED
PESAARKFREEIQTYKTG
3D structure
PDB1g4p Structural characterization of the enzyme-substrate, enzyme-intermediate, and enzyme-product complexes of thiamin phosphate synthase.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R1059 A1130
Catalytic site (residue number reindexed from 1) R50 A121
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 D84 D103
BS02 FQP B Y1029 Q1057 R1059 K1061 N1092 D1093 H1107 G1109 A1130 I1186 S1206 Y20 Q48 R50 K52 N83 D84 H98 G100 A121 I170 S190
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:1g4p, PDBe:1g4p, PDBj:1g4p
PDBsum1g4p
PubMed11513589
UniProtP39594|THIE_BACSU Thiamine-phosphate synthase (Gene Name=thiE)

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