Structure of PDB 1iig Chain B

Receptor sequence
>1iigB (length=249) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMT
KERLSHPKFVIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAY
YGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIA
KKLKKADWAKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGAD
VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ
3D structure
PDB1iig The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three different complexes.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N311 K313 H395 E397 E467 G473 S513
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 3PP B K313 H395 E467 I472 G473 S513 G534 K12 H94 E166 I171 G172 S212 G233 PDBbind-CN: -logKd/Ki=1.57,Ki=27mM
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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Biological Process
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Cellular Component
External links
PDB RCSB:1iig, PDBe:1iig, PDBj:1iig
PDBsum1iig
PubMed2062828
UniProtP04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal

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