Structure of PDB 5tk3 Chain A

Receptor sequence
>5tk3A (length=349) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
SGYGLPISQEVAKELAENARKIAAPGKGILAADESTGTIKKRFDSIGVEN
TEANRAFYRDLLFSTKGLGQYISGAILFEETLYQKSPSGVPMVDLLKAEG
IIPGIKVDKGLETLPLTDDEKATMGLDGLSERCKKYYEAGARFAKWRAVL
SIDPAKGKPTNLSITEVAHGLARYAAICQANRLVPIVEPEILTDGSHDIT
VCAEVTERVLAAVFKALNDHHVLLEGALLKPNMVTHGSDCPKPASHEEIA
FYTVRSLKRTVPPALPGVMFLSGGQSEEDASLNLNEMNKMGPHPFQLSFS
YGRALQASCLKAWKGVPENKAKAQQVLMERARANGEAQLGKYGGGAYVY
3D structure
PDB5tk3 Isomer activation controls stereospecificity of class I fructose-1,6-bisphosphate aldolases.
ChainA
Resolution1.83 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D34 K146 E189 E191 K231 S301 Y363
Catalytic site (residue number reindexed from 1) D33 K145 E188 E190 K230 S300 Y349
Enzyme Commision number 4.1.2.13: fructose-bisphosphate aldolase.
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 G3H A S36 K107 K146 R148 E189 S35 K106 K145 R147 E188
Gene Ontology
Molecular Function
GO:0003779 actin binding
GO:0004332 fructose-bisphosphate aldolase activity
GO:0016829 lyase activity
Biological Process
GO:0006096 glycolytic process
GO:0030388 fructose 1,6-bisphosphate metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5tk3, PDBe:5tk3, PDBj:5tk3
PDBsum5tk3
PubMed28972169
UniProtQ8I8I2|ALF1_TOXGO Fructose-bisphosphate aldolase 1 (Gene Name=ald-1)

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