Structure of PDB 6ooi Chain A

Receptor sequence
>6ooiA (length=250) Species: 6183 (Schistosoma mansoni) [Search protein sequence]
SRKFFVGGNWKMNGSRDDNDKLLKLLSEAHFDDNTEVLIAPPSVFLHEIR
KSLKKEIHVAAQNCYKVSKGAFTGEISPAMIRDIGCDWVILGHSERRNIF
GESDELIAEKVQHALAEGLSVIACIGETLSERESNKTEEVCVRQLKAIAN
KIKSADEWKRVVVAYEPVWAIGTGKVATPQQAQEVHNFLRKWFKTNAPNG
VDEKIRIIYGGSVTAANCKELAQQHDVDGFLVGGASLKPEFTEICKARQR
3D structure
PDB6ooi Crystal structures of Triosephosphate Isomerases from Taenia solium and Schistosoma mansoni provide insights for vaccine rationale and drug design against helminth parasites.
ChainA
Resolution2.14 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) N12 K14 H96 E98 E169 G175 S215
Catalytic site (residue number reindexed from 1) N9 K11 H93 E95 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 K14 H96 E169 I174 G175 G214 S215 G236 G237 K11 H93 E166 I171 G172 G211 S212 G233 G234
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6ooi, PDBe:6ooi, PDBj:6ooi
PDBsum6ooi
PubMed31923219
UniProtP48501|TPIS_SCHMA Triosephosphate isomerase (Gene Name=TPI)

[Back to BioLiP]