Structure of PDB 1tpu Chain B

Receptor sequence
>1tpuB (length=245) Species: 9031 (Gallus gallus) [Search protein sequence]
RKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFARQ
KLDAKIGVAAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGNSERRHVFG
ESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADN
VKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVSDAVAQS
TRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDIINAKH
3D structure
PDB1tpu The structural basis for pseudoreversion of the H95N lesion by the secondary S96P mutation in triosephosphate isomerase.
ChainB
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N11 K13 N95 E97 E165 G171 S211
Catalytic site (residue number reindexed from 1) N8 K10 N92 E94 E162 G168 S208
Enzyme Commision number 4.2.3.3: methylglyoxal synthase.
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 PGH B K13 E165 I170 G171 G209 S211 L230 G232 G233 K10 E162 I167 G168 G206 S208 L227 G229 G230
Gene Ontology
Molecular Function
GO:0004807 triose-phosphate isomerase activity
GO:0008929 methylglyoxal synthase activity
GO:0016829 lyase activity
GO:0016853 isomerase activity
GO:0031625 ubiquitin protein ligase binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006006 glucose metabolic process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0019242 methylglyoxal biosynthetic process
GO:0019563 glycerol catabolic process
GO:0019682 glyceraldehyde-3-phosphate metabolic process
GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
GO:0061621 canonical glycolysis
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1tpu, PDBe:1tpu, PDBj:1tpu
PDBsum1tpu
PubMed8952501
UniProtP00940|TPIS_CHICK Triosephosphate isomerase (Gene Name=TPI1)

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