Structure of PDB 8eq0 Chain A

Receptor sequence

>8eq0A (length=462) Species: 562 (Escherichia coli)

MKKTKIVCTIGPKTESEEMLAKMLDAGMNVMRLNFSHGDYAEHGQRIQNL
RNVMSKTGKTAAILLDTKGPEIRTMKLEGGNDVSLKAGQTFTFTTDKSVI
GNSEMVAVTYEGFTTDLSVGNTVLVDDGLIGMEVTAIEGNKVICKVLNNG
DLGENKGVNLPGVSIALPALAEKDKQDLIFGCEQGVDFVAASFIRKRSDV
IEIREHLKAHGGENIHIISKIENQEGLNNFDEILEASDGIMVARGDLGVE
IPVEEVIFAQKMMIEKCIRARKVVITATQMLDSMIKNPRPTRAEAGDVAN
AILDGTDAVMLSGESAKGKYPLEAVSIMATICERTDRVMNSRLERITEAV
CRGAVETAEKLDAPLIVVATQGAKSARAVRKYFPDATILALTTNEKTAHQ
LVLSKGVVPQLVKEITSTDDFYRLGKELALQSGLAHKGDVVVMVSGALVP
SGTTNTASVHVL

3D structure

• PDB: 8eq0 Beneficial mutations occurring in E. coli pyruvate kinase afford new allosteric mechanisms leading to faster resumption of growth
• Chain: A
• Resolution: 2.62 Å

Enzymatic activity

• 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	GLY	A	E235 A236 S237 K272	E235 A236 S237 K272

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0003824 catalytic activity
• GO:0004743 pyruvate kinase activity
• GO:0005515 protein binding
• GO:0005524 ATP binding
• GO:0016301 kinase activity
• GO:0030955 potassium ion binding
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006096 glycolytic process
• GO:0009408 response to heat
• GO:0016310 phosphorylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0016020 membrane
• GO:1902912 pyruvate kinase complex

External links

• PDB: RCSB:8eq0, PDBe:8eq0, PDBj:8eq0
• PDBsum: 8eq0
• UniProt: P0AD61|KPYK1_ECOLI Pyruvate kinase I (Gene Name=pykF)