Structure of PDB 6su2 Chain A Binding Site BS02

Receptor Information

>6su2 Chain A (length=498) Species: 1068625 (Trypanosoma congolense IL3000)

SQLQHNIGLSIFEPVAKHRANRIICTIGPSTQSVEALKGLMKSGMSVARM
NFSHGSYEYHQTTINNVRAAAAELGLHIGIALDTKGPEIRTGLFKDGEAT
YAPGDTVLVTTDPAFEKIGTKEKFYVDYPQLPNVVRPGGLIYVDDGVLTL
RVLSKEDDCTLKCHVNNHHRLTDRKGINLPGCEVDLPAVSEKDRKDLQFG
VEQGVDMIFASFIRTADQVREVRAALGEKGKDTLIISKIENHQGVQNIDA
IIEASDGIMVARGDLGVEIPAEKVVVAQMCIISKCNVAGKPVICATQMLE
SMTTNPRPTRAEVTDVANAVFNGADCVMLSGETAKGKYPNEVVQYMVRIC
IEAQSATHDSVMFNSIKNLQKIPMSPEEAVCSSAVSSAFEVQAKAILVLS
NTGRSARLISKYRPNCPIICATTRLLTCRQLNVTRSVESVYYDVDAHGED
NDREKRVQLGVDWAKTKGYVSAGDVMVIVHADHSVKGYPNQTRLVRVR

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 6su2 Chain A Residue 602

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6su2 Structural and kinetic characterization of Trypanosoma congolense pyruvate kinase.
• Resolution: 3.0 Å
• Binding residue (original residue number in PDB): E241 D265
• Binding residue (residue number reindexed from 1): E240 D264
• Annotation score: 1

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.

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

External links

• PDB: RCSB:6su2, PDBe:6su2, PDBj:6su2
• PDBsum: 6su2
• PubMed: 32084384
• UniProt: G0UYF4