Structure of PDB 1kv5 Chain B

Receptor sequence
>1kv5B (length=249) Species: 5702 (Trypanosoma brucei brucei) [Search protein sequence]
SKPQPIAAANWKCNGSQQSLSELIDLFNSTSINHDVQCVVASTFVHLAMT
KERLSHPKFVIAAQNAIAKSGAFTGEVSLPILKDFGVNWIVLGHSERRAY
YGETNEIVADKVAAAVASGFMVIACIGETLQERESGRTAVVVLTQIAAIA
KKLKKADWAKVVIAYEPVWAIGTGKVATPQQAQEAHALISSWVSSKIGAD
VAGELRILYGGSVNGKNARTLYQQRDVNGFLVGGASLKPEFVDIIKATQ
3D structure
PDB1kv5 The importance of the conserved Arg191-Asp227 salt bridge of triosephosphate isomerase for folding, stability, and catalysis
ChainB
Resolution1.65 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 B K13 H95 E167 I172 G212 S213 G234 G235 K12 H94 E166 I171 G211 S212 G233 G234 MOAD: Ki=60uM
PDBbind-CN: -logKd/Ki=4.22,Ki=60uM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1kv5, PDBe:1kv5, PDBj:1kv5
PDBsum1kv5
PubMed11997014
UniProtP04789|TPIS_TRYBB Triosephosphate isomerase, glycosomal

[Back to BioLiP]