Structure of PDB 2wsr Chain A

Receptor sequence
>2wsrA (length=242) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVAPRFVMIAMT
KERLSHPKFVIAAQNAGNADGLASLKDFGVNWIVLGHSERRAYYGETNEI
VADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKAD
WAKVVIAYEPVWAIGTGKVATPQQAQETHALIRSWVSSKIGADVAGELRI
LYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ
3D structure
PDB2wsr Space Group Transition Driven by Temperature and Related to Monomer-Dimer Transition in Solution: The Case of Monomeric Tim of Trypanosoma Brucei Brucei
ChainA
Resolution1.65 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 H87 E89 E159 G165 S205
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 AZI A I33 H57 I32 H56
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:2wsr, PDBe:2wsr, PDBj:2wsr
PDBsum2wsr
PubMed
UniProtP04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal

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