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Structure of PDB 1btm Chain B

Receptor sequence >1btmB (length=251) Species: 1422 (Geobacillus stearothermophilus) [Search protein sequence] RKPIIAGNWKMHKTLAEAVQFVEDVKGHVPPADEVISVVCAPFLFLDRLV QAADGTDLKIGAQTMHFADQGAYTGEVSPVMLKDLGVTYVILGHSERRQM FAETDETVNKKVLAAFTRGLIPIICCGESLEEREAGQTNAVVASQVEKAL AGLTPEQVKQAVIAYEPIWAIGTGKSSTPEDANSVCGHIRSVVSRLFGPE AAEAIRIQYGGSVKPDNIRDFLAQQQIDGPLVGGASLEPASFLQLVEAGR H

3D structure PDB 1btm Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interactions. Chain B Resolution 2.8 Å 3D structure Catalytic site residues are labeled in the structure [Spin on] [Spin off] [Reset orientation] [High quality] [Low quality] [White background] [Black background] [Download] [Download structure with residue number starting from 1]

Enzymatic activity Catalytic site (original residue number in PDB) N8 K10 H94 E96 E166 G172 S212 Catalytic site (residue number reindexed from 1) N8 K10 H94 E96 E166 G172 S212 Enzyme Commision number 5.3.1.1: triose-phosphate isomerase.

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 PGA B K10 H94 E166 I171 G172 G211 S212 G233 K10 H94 E166 I171 G172 G211 S212 G233

Gene Ontology Molecular Function GO:0004807 triose-phosphate isomerase activity GO:0016853 isomerase activity

	Biological Process
GO:0006094	gluconeogenesis
GO:0006096	glycolytic process
GO:0019563	glycerol catabolic process
GO:0046166	glyceraldehyde-3-phosphate biosynthetic process

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol

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