Structure of PDB 6v74 Chain A

Receptor sequence
>6v74A (length=513) Species: 9606 (Homo sapiens) [Search protein sequence]
QTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKE
MIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALD
TKGPEIRTGLIKGVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVV
EVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDL
PAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKII
SKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCN
RAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKG
DYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVE
ASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRG
IFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPG
SGFTNTMRVVPVP
3D structure
PDB6v74 Biochemical and structural insights into how amino acids regulate pyruvate kinase muscle isoform 2.
ChainA
Resolution2.32 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) R60 R107 K252 T310
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 A K270 A293 G295 D296 T328 K252 A275 G277 D278 T310
BS02 FBP A L431 T432 K433 S434 S437 W482 R489 G514 R516 P517 G518 S519 G520 F521 T522 L413 T414 K415 S416 S419 W464 R471 G496 R498 P499 G500 S501 G502 F503 T504
BS03 MG A E272 D296 E254 D278
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:6v74, PDBe:6v74, PDBj:6v74
PDBsum6v74
PubMed32144209
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

[Back to BioLiP]