Structure of PDB 6v74 Chain B

Receptor sequence
>6v74B (length=516) Species: 9606 (Homo sapiens) [Search protein sequence]
QQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMI
KSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTK
GPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNIC
KVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAA
VDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNI
KIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIG
RCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGET
AKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVG
AVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHL
YRGIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGW
RPGSGFTNTMRVVPVP
3D structure
PDB6v74 Biochemical and structural insights into how amino acids regulate pyruvate kinase muscle isoform 2.
ChainB
Resolution2.32 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) R58 R105 K255 T313
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 B K270 E272 A293 G295 D296 T328 K255 E257 A278 G280 D281 T313
BS02 FBP B L431 T432 K433 S434 S437 W482 R489 G514 R516 P517 G518 S519 G520 F521 T522 L416 T417 K418 S419 S422 W467 R474 G499 R501 P502 G503 S504 G505 F506 T507
BS03 MG B E272 D296 E257 D281
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:6v74, PDBe:6v74, PDBj:6v74
PDBsum6v74
PubMed32144209
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

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