Structure of PDB 2vel Chain B

Receptor sequence
>2velB (length=238) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
SKPQPIAAANWKSGSPDSLSELIDLFNSTSINHDVQCVVASTFVHLAMTK
ERLSHPKFVIAAQNAGNADALASLKDFGVNWIVLGHSERRWYYGETNEIV
ADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIAKKLKKADW
AKVVIAYEPVWAIGTGKVATPQQAQEAHALIRSWVSSKIGADVAGELRIL
YGGSVNGKNARTLYQQRDVNGFLAGLKPEFVDIIKATQ
3D structure
PDB2vel Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties.
ChainB
Resolution2.3 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 H86 E88 E158 G164 S204
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 B K13 H95 E167 I172 G173 G212 S213 A233 G234 K12 H86 E158 I163 G164 G203 S204 A224 G225
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:2vel, PDBe:2vel, PDBj:2vel
PDBsum2vel
PubMed18239072
UniProtP04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal

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