Structure of PDB 4jpg Chain D

Receptor sequence
>4jpgD (length=512) Species: 9606 (Homo sapiens) [Search protein sequence]
QTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKE
MIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALD
TKGPEIRTGLITAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKV
VEVGSKIYVDDGLISLQVKQKDFLVTEVENGGSLGSKKGVNLPGAAVDLP
AVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIIS
KIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNR
AGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGD
YPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEA
SFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGI
FPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGS
GFTNTMRVVPVP
3D structure
PDB4jpg Discovery of 2-((1H-benzo[d]imidazol-1-yl)methyl)-4H-pyrido[1,2-a]pyrimidin-4-ones as novel PKM2 activators.
ChainD
Resolution2.33 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 K251 T309
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 FBP D L431 T432 K433 S434 S437 W482 R489 G514 R516 P517 G518 S519 F521 T522 L412 T413 K414 S415 S418 W463 R470 G495 R497 P498 G499 S500 F502 T503
BS02 1OX D F26 K311 Q393 F13 K292 Q374
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:4jpg, PDBe:4jpg, PDBj:4jpg
PDBsum4jpg
PubMed23622982
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

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