Structure of PDB 5tkl Chain A

Receptor sequence
>5tklA (length=350) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
MSGYGLPISQEVAKELAENARKIAAPGKGILAADESTGTIKKRFDSIGVE
NTEANRAFYRDLLFSTKGLGQYISGAILFEETLYQKSPSGVPMVDLLKAE
GIIPGIKVDKGLETLPLTDDEKATMGLDGLSERCKKYYEAGARFAKWRAV
LSIDPAKGKPTNLSITEVAHGLARYAAICQANRLVPIVEPEILTDGSHDI
TVCAEVTERVLAAVFKALNDHHVLLEGALLKPNMVTHGSDCPKPASHEEI
AFYTVRSLKRTVPPALPGVMFLSGGQSEEDASLNLNEMNKMGPHPFQLSF
SYGRALQASCLKAWKGVPENKAKAQQVLMERARANGEAQLGKYGGGAYVY
3D structure
PDB5tkl Isomer activation controls stereospecificity of class I fructose-1,6-bisphosphate aldolases.
ChainA
Resolution1.751 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) D34 K146 E189 E191 K231 S301 Y350
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 P6F A A32 D34 S36 T39 K107 K146 R148 E189 K231 S273 G274 G303 R304 A32 D34 S36 T39 K107 K146 R148 E189 K231 S273 G274 G303 R304
BS02 G3H A S36 T39 K107 K146 R148 E189 K231 S36 T39 K107 K146 R148 E189 K231
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:5tkl, PDBe:5tkl, PDBj:5tkl
PDBsum5tkl
PubMed28972169
UniProtQ8I8I2|ALF1_TOXGO Fructose-bisphosphate aldolase 1 (Gene Name=ald-1)

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