Structure of PDB 1tpc Chain 2

Receptor sequence
>1tpc2 (length=245) Species: 9031 (Gallus gallus) [Search protein sequence]
RKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFARQ
KLDAKIGVAAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHPERRHVFG
ESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKAIADN
VKDWSKVVLAYDPVWAIGTGKTATPQQAQEVHEKLRGWLKTHVSDAVAQS
TRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDIINAKH
3D structure
PDB1tpc The structural basis for pseudoreversion of the E165D lesion by the secondary S96P mutation in triosephosphate isomerase depends on the positions of active site water molecules.
Chain2
Resolution1.9 Å
3D
structure
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Enzymatic activity
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 2 K13 H95 D165 I170 G171 G210 S211 L230 G232 K10 H92 D162 I167 G168 G207 S208 L227 G229
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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Cellular Component
External links
PDB RCSB:1tpc, PDBe:1tpc, PDBj:1tpc
PDBsum1tpc
PubMed7577950
UniProtP00940|TPIS_CHICK Triosephosphate isomerase (Gene Name=TPI1)

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