Structure of PDB 3pvf Chain A

Receptor sequence
>3pvfA (length=246) Species: 5833 (Plasmodium falciparum) [Search protein sequence]
RKYFVAANWKCNGTLESIKSLTNSFNNLDFDPSKLDVVVFPVSVHYDHTR
KLLQSKFSTGIQNVSKFGNGSYTGEVSAEIAKDLNIEYVIIGHFERRKYF
HETDEDVREKLQASLKNNLKAVVSFGESLEQREQNKTIEVITKQVKAFVD
LIDNFDNVILVYEPLWAIGTGKTATPEQAQLVHKEIRKIVKDTCGEKQAN
QIRILYGGSVNTENCSSLIQQEDIDGFLVGNASLKESFVDIIKSAM
3D structure
PDB3pvf Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stability.
ChainA
Resolution1.73 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 PGA A K12 H95 E165 I170 G171 G210 S211 L230 G232 N233 K10 H93 E163 I168 G169 G208 S209 L228 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:3pvf, PDBe:3pvf, PDBj:3pvf
PDBsum3pvf
PubMed21447068
UniProtQ07412|TPIS_PLAFA Triosephosphate isomerase (Gene Name=TPI)

[Back to BioLiP]