Structure of PDB 6p0y Chain B

Receptor sequence
>6p0yB (length=500) Species: 353152 (Cryptosporidium parvum Iowa II) [Search protein sequence]
GKATCLGMDKICSPLNDVTQRKTQIICTIGPSCNNVESLIGLIDKGMSVA
RLNFSHGDHESHFKTLQNIREAAKARPHSTVGIMLDTKGPEIRTGMLEGG
KPLKAGQTLKITTDYSMLGNSECISCSYSLLPKSVQIGSTVLIADGSLST
QVLEIGDDFIVCKVLNSVTIGERKNMNLPGCVHLPIIGDKDRHDIVDFAL
KYNLDFIALSFVQNGADVQLCRQIISENTQYSNGIPSSIKIISKIENLEG
VINFDSICSESDGIMVARGDLGMEIPPEKIFVAQKCMISKCNVAGKPVVT
ATQMLESMIKSNRPTRAEMTDVANAVLDGSDCVMLSGETANGAFPFDAVN
VMSRVCAQAETCIDYPVLYHAIHSSVPKPVAVPEAIACSAVESAHDVNAK
LIITITETGNTARLISKYRPSQTIIACTAKPEVARGLKIARGVKTYVLNS
IHHSEVVISNALALAKEESLIESGDFAIAVHGVKESCPGSCNLMKIVRCP
3D structure
PDB6p0y An overview of structure, function, and regulation of pyruvate kinases.
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R74 R116 K270 T328
Catalytic site (residue number reindexed from 1) R51 R93 K244 T302
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 ADP B P54 N76 H79 R116 S362 A366 N367 P31 N53 H56 R93 S336 A340 N341
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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Cellular Component
External links
PDB RCSB:6p0y, PDBe:6p0y, PDBj:6p0y
PDBsum6p0y
PubMed31342570
UniProtQ5CSM7

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