Structure of PDB 4yng Chain E

Receptor sequence
>4yngE (length=470) Species: 562 (Escherichia coli) [Search protein sequence]
MKKTKIVCTIGPKTESEEMLAKMLDAGMNVMRLNFSHGDYAEHGQRIQNL
RNVMSKTGKTAAILLDTKGPEIRTMKLEGGNDVSLKAGQTFTFTTDKSVI
GNSEMVAVTYEGFTTDLSVGNTVLVDDGLIGMEVTAIEGNKVICKVLNNG
DLGENKGVNLPGVSIALPALAEKDKQDLIFGCEQGVDFVAASFIRKRSDV
IEIREHLKAHGGENIHIISKIENQEGLNNFDEILEASDGIMVARGDLGVE
IPVEEVIFAQKMMIEKCIRARKVVITATQMLDSMIKNPRPTRAEAGDVAN
AILDGTDAVMLSGESAKGKYPLEAVSIMATICERTDRVMNSRLEFNNDNR
KLRITEAVCRGAVETAEKLDAPLIVVATQGGKSARAVRKYFPDATILALT
TNEKTAHQLVLSKGVVPQLVKEITSTDDFYRLGKELALQSGLAHKGDVVV
MVSGALVPSGTTNTASVHVL
3D structure
PDB4yng Grappling with anisotropic data, pseudo-merohedral twinning and pseudo-translational noncrystallographic symmetry: a case study involving pyruvate kinase.
ChainE
Resolution2.28 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R32 R73 K220 T278
Catalytic site (residue number reindexed from 1) R32 R73 K220 T278
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 SO4 E T378 Q379 G380 S383 G460 T378 Q379 G380 S383 G460
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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Cellular Component
External links
PDB RCSB:4yng, PDBe:4yng, PDBj:4yng
PDBsum4yng
PubMed27050130
UniProtP0AD62|KPYK1_ECO57 Pyruvate kinase I (Gene Name=pykF)

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