Structure of PDB 1wob Chain D

Receptor sequence
>1wobD (length=246) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
RKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTR
KLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYF
HETDEDVREKLQASLKNNLKAVVCFGESLEQREQNKTIEVITKQVKAFVD
LIDNFDNVILVYEPLFAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQAN
QIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM
3D structure
PDB1wob Structures of Unliganded and Inhibitor Complexes of W168F, a Loop6 Hinge Mutant of Plasmodium falciparum Triosephosphate Isomerase: Observation of an Intermediate Position of Loop6
ChainD
Resolution2.8 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) N10 K12 H95 E97 E165 G171 S211
Catalytic site (residue number reindexed from 1) N8 K10 H93 E95 E163 G169 S209
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 SO4 D S211 G232 N233 S209 G230 N231
Gene Ontology
Molecular Function
GO:0004807 triose-phosphate isomerase activity
GO:0016853 isomerase activity
GO:0042802 identical protein binding
Biological Process
GO:0006094 gluconeogenesis
GO:0006096 glycolytic process
GO:0019563 glycerol catabolic process
GO:0046166 glyceraldehyde-3-phosphate biosynthetic process
Cellular Component
GO:0005829 cytosol

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1wob, PDBe:1wob, PDBj:1wob
PDBsum1wob
PubMed15465054
UniProtQ07412|TPIS_PLAFA Triosephosphate isomerase (Gene Name=TPI)

[Back to BioLiP]