Structure of PDB 6nu5 Chain B

Receptor sequence
>6nu5B (length=518) Species: 9606 (Homo sapiens) [Search protein sequence]
QTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKE
MIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALD
TKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKN
ICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPG
AAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGK
NIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMM
IGRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSG
ETAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATA
VGAVEASFKCCSGAIIVLTKSGRYAHQVARYRPRAPIIAVTRNPQTARQA
HLYRGIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLT
GWRPGSGFTNTMRVVPVP
3D structure
PDB6nu5 Mechanistic and Structural Insights into Cysteine-Mediated Inhibition of Pyruvate Kinase Muscle Isoform 2.
ChainB
Resolution1.6 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 K257 T315
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 CYS B R43 N44 N70 H464 I469 F470 R30 N31 N57 H451 I456 F457
BS02 OXL B K270 E272 A293 G295 D296 T328 K257 E259 A280 G282 D283 T315
BS03 MG B E272 D296 E259 D283
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:6nu5, PDBe:6nu5, PDBj:6nu5
PDBsum6nu5
PubMed31386812
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

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