Structure of PDB 6ksh Chain A

Receptor sequence
>6kshA (length=490) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
GASMQSAANITLRQILEPNNVNLRSKKTHIVCTLGPACKSVETLVKLIDA
GMDICRFNFSHGSHEDHKEMFNNVLKAQELRPNCLLGMLLDTKGPEIRTG
FLKNKEVHLKEGSKLKLVTDYEFLGDETCIACSYKKLPQSVKPGNIILIA
DGSVSCKVLETHEDHVITEVLNSAVIGERKNMNLPNVKVDLPIISEKDKN
DILNFAIPMGCNFIAASFIQSADDVRLIRNLLGPRGRHIKIIPKIENIEG
IIHFDKILAESDGIMIARGDLGMEISPEKVFLAQKLMISKCNLQGKPIIT
ATQMLESMTKNPRPTRAEVTDVANAVLDGTDCVMLSGETAGGKFPVEAVT
IMSKICLEAEACIDYKLLYQSLVNAIETPISVQEAVARSAVETAESIQAS
LIIALTETGYTARLIAKYKPSCTILALSASDSTVKCLNVHRGVTCIKVGS
FQGTDIVIRNAIEIAKQRNMAKVGDSVIAIHNLMKVVQIE
3D structure
PDB6ksh Pyruvate kinase from Plasmodium falciparum: Structural and kinetic insights into the allosteric mechanism.
ChainA
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) R67 R109 K255 T313
Catalytic site (residue number reindexed from 1) R56 R98 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 MG A E257 D281 E246 D270
BS02 ATP A P47 R67 N69 H72 R109 K191 S347 G348 P36 R56 N58 H61 R98 K180 S336 G337
BS03 OXL A K255 E257 A278 G280 D281 T313 K244 E246 A267 G269 D270 T302
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
GO:0051289 protein homotetramerization
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:6ksh, PDBe:6ksh, PDBj:6ksh
PDBsum6ksh
PubMed32878705
UniProtC6KTA4

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