Structure of PDB 2j27 Chain A

Receptor sequence
>2j27A (length=249) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMT
KERLSHPKFVIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAY
YGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIA
KKLKKADWAKVVIAYEAVWAIGTGKVATPQQAQEAHALIRSWVSSKIGAD
VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ
3D structure
PDB2j27 Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase.
ChainA
Resolution1.15 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 E167 G173 S213
Catalytic site (residue number reindexed from 1) N10 K12 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 A K13 H95 E167 I172 G212 S213 G234 G235 K12 H94 E166 I171 G211 S212 G233 G234 MOAD: Ki=0.3mM
PDBbind-CN: -logKd/Ki=3.52,Ki=0.3mM
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
GO:0020015 glycosome

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Cellular Component
External links
PDB RCSB:2j27, PDBe:2j27, PDBj:2j27
PDBsum2j27
PubMed17176070
UniProtP04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal

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