Structure of PDB 4thi Chain A

Receptor sequence
>4thiA (length=362) Species: 1423 (Bacillus subtilis) [Search protein sequence]
ITLKVAIYPYVPDPARFQAAVLDQWQRQEPGVKLEFTDWDSYSADPPDDL
DVFVLDSIFLSHFVDAGYLLPFGSQDIDQAEDVLPFALQGAKRNGEVYGL
PQILCTNLLFYRKGDLKIGQVDNIYELYKKIGTSHSEQIPPPQNKGLLIN
MAGGTTKASMYLEALIDVTGQYTEYDLLPPLDPLNDKVIRGLRLLINMAG
EKPSQYVPEDGDAYVRASWFAQGSGRAFIGYSESMMRMGDYAEQVRFKPI
SSSAGQDIPLFYSDVVSVNSKTAHPELAKKLANVMASADTVEQALRPQAD
GQYPQYLLPARHQVYEALMQDYPIYSELAQIVNKPSNRVFRLGPEVRTWL
KDAKQVLPEALG
3D structure
PDB4thi Crystal structure of thiaminase-I from Bacillus thiaminolyticus at 2.0 A resolution.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) C113 E241 D272
Catalytic site (residue number reindexed from 1) C105 E233 D264
Enzyme Commision number 2.5.1.2: thiamine pyridinylase.
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 PYD A Y18 C113 Y239 Y270 Y10 C105 Y231 Y262
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0050332 thiamine pyridinylase activity
Biological Process
GO:0009230 thiamine catabolic process
Cellular Component
GO:0005576 extracellular region

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4thi, PDBe:4thi, PDBj:4thi
PDBsum4thi
PubMed9843405
UniProtP45741|THI1_PANTH Thiaminase-1

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