Structure of PDB 1sw0 Chain A

Receptor sequence
>1sw0A (length=247) Species: 9031 (Gallus gallus) [Search protein sequence]
APRKFFVGGNWKMNGDKKSLGELIHTLNGAKLSADTEVVCGAPSIYLDFA
RQKLDAKIGVAAQNCYKVPKGAFTGEISPAMIKDIGAAWVILGHSERRHV
FGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKVVFEQTKAIA
DNVKDWSKVVLAYEPVWAIGTGLWATPQQAQEVHEKLRGWLKSHVSDAVA
QSTRIIYGGSVTGGNCKELASQHDVDGFLVGGASLKPEFVDIINAKH
3D structure
PDB1sw0 Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase
ChainA
Resolution1.71 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 H95 E97 E165 G171 S211
Catalytic site (residue number reindexed from 1) N10 K12 H94 E96 E164 G170 S210
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 PGA A K13 H95 E165 I170 G171 S211 G232 G233 K12 H94 E164 I169 G170 S210 G231 G232
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:1sw0, PDBe:1sw0, PDBj:1sw0
PDBsum1sw0
PubMed15166315
UniProtP00940|TPIS_CHICK Triosephosphate isomerase (Gene Name=TPI1)

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