Structure of PDB 3me3 Chain B

Receptor sequence
>3me3B (length=498) Species: 9606 (Homo sapiens) [Search protein sequence]
QTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKE
MIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALD
TKGPEIRTGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDD
GLISLQVDFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGV
EQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEI
LEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQMLES
MIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQHLIAR
EAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVLTK
SGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQEAWA
EDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
3D structure
PDB3me3 Pyruvate kinase M2 activators promote tetramer formation and suppress tumorigenesis.
ChainB
Resolution1.95 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R73 R120 K270 T328
Catalytic site (residue number reindexed from 1) R60 R107 K237 T295
Enzyme Commision number 2.7.10.2: non-specific protein-tyrosine kinase.
2.7.11.1: non-specific serine/threonine protein kinase.
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 3SZ B F26 L27 Y390 Q393 L394 F13 L14 Y357 Q360 L361 BindingDB: EC50=38nM
BS02 FBP B L431 T432 K433 S434 S437 W482 R489 G514 R516 P517 G518 S519 G520 F521 T522 L398 T399 K400 S401 S404 W449 R456 G481 R483 P484 G485 S486 G487 F488 T489
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0003824 catalytic activity
GO:0004713 protein tyrosine kinase activity
GO:0004743 pyruvate kinase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0023026 MHC class II protein complex binding
GO:0030955 potassium ion binding
GO:0045296 cadherin binding
GO:0046872 metal ion binding
Biological Process
GO:0006096 glycolytic process
GO:0006417 regulation of translation
GO:0012501 programmed cell death
GO:0016310 phosphorylation
GO:0032869 cellular response to insulin stimulus
GO:0061621 canonical glycolysis
GO:1903672 positive regulation of sprouting angiogenesis
GO:2000767 positive regulation of cytoplasmic translation
Cellular Component
GO:0005576 extracellular region
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005791 rough endoplasmic reticulum
GO:0005829 cytosol
GO:0005929 cilium
GO:0031982 vesicle
GO:0034774 secretory granule lumen
GO:0062023 collagen-containing extracellular matrix
GO:0070062 extracellular exosome
GO:1903561 extracellular vesicle
GO:1904813 ficolin-1-rich granule lumen

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3me3, PDBe:3me3, PDBj:3me3
PDBsum3me3
PubMed22922757
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

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