Structure of PDB 4fxf Chain C

Receptor sequence
>4fxfC (length=500) Species: 9606 (Homo sapiens) [Search protein sequence]
RLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTH
EYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAE
VELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLI
SLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKF
GVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFD
EILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAGKPVICATQML
ESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYPLEAVRMQNLI
AREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASFKCCSGAIIVL
TKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFPVLCKDPVQEA
WAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGFTNTMRVVPVP
3D structure
PDB4fxf M2 pyruvate kinase provides a mechanism for nutrient sensing and regulation of cell proliferation.
ChainC
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R73 R120 K270 T328
Catalytic site (residue number reindexed from 1) R42 R89 K239 T297
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 OXL C K270 A293 G295 D296 T328 K239 A262 G264 D265 T297
BS02 MG C E272 D296 E241 D265
BS03 FBP C L431 T432 K433 S434 S437 R489 G514 R516 P517 G518 S519 F521 L400 T401 K402 S403 S406 R458 G483 R485 P486 G487 S488 F490
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4fxf, PDBe:4fxf, PDBj:4fxf
PDBsum4fxf
PubMed23530218
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

[Back to BioLiP]