Structure of PDB 6su2 Chain A

Receptor sequence
>6su2A (length=498) Species: 1068625 (Trypanosoma congolense IL3000) [Search protein sequence]
SQLQHNIGLSIFEPVAKHRANRIICTIGPSTQSVEALKGLMKSGMSVARM
NFSHGSYEYHQTTINNVRAAAAELGLHIGIALDTKGPEIRTGLFKDGEAT
YAPGDTVLVTTDPAFEKIGTKEKFYVDYPQLPNVVRPGGLIYVDDGVLTL
RVLSKEDDCTLKCHVNNHHRLTDRKGINLPGCEVDLPAVSEKDRKDLQFG
VEQGVDMIFASFIRTADQVREVRAALGEKGKDTLIISKIENHQGVQNIDA
IIEASDGIMVARGDLGVEIPAEKVVVAQMCIISKCNVAGKPVICATQMLE
SMTTNPRPTRAEVTDVANAVFNGADCVMLSGETAKGKYPNEVVQYMVRIC
IEAQSATHDSVMFNSIKNLQKIPMSPEEAVCSSAVSSAFEVQAKAILVLS
NTGRSARLISKYRPNCPIICATTRLLTCRQLNVTRSVESVYYDVDAHGED
NDREKRVQLGVDWAKTKGYVSAGDVMVIVHADHSVKGYPNQTRLVRVR
3D structure
PDB6su2 Structural and kinetic characterization of Trypanosoma congolense pyruvate kinase.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R50 R91 K239 T297
Catalytic site (residue number reindexed from 1) R49 R90 K238 T296
Enzyme Commision number 2.7.1.40: pyruvate kinase.
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 FBP A L400 S401 N402 T403 R405 S406 R454 R457 G488 Y489 P490 L399 S400 N401 T402 R404 S405 R453 R456 G487 Y488 P489
BS02 MG A E241 D265 E240 D264
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003824 catalytic activity
GO:0004743 pyruvate kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0030955 potassium ion binding
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
GO:0016310 phosphorylation
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6su2, PDBe:6su2, PDBj:6su2
PDBsum6su2
PubMed32084384
UniProtG0UYF4

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