Structure of PDB 6v75 Chain C Binding Site BS03

Receptor Information
>6v75 Chain C (length=517) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEM
IKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDT
KGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNI
CKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGA
AVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKN
IKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMI
GRCNRAGKPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGE
TAKGDYPLEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAV
GAVEASFKCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAH
LYRGIFPVLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTG
WRPGSGFTNTMRVVPVP
Ligand information
Ligand IDOXL
InChIInChI=1S/C2H2O4/c3-1(4)2(5)6/h(H,3,4)(H,5,6)/p-2
InChIKeyMUBZPKHOEPUJKR-UHFFFAOYSA-L
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341		[O-]C(=O)C([O-])=O
OpenEye OEToolkits 1.5.0C(=O)(C(=O)[O-])[O-]
FormulaC2 O4
NameOXALATE ION
ChEMBL
DrugBank
ZINC
PDB chain6v75 Chain C Residue 609 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6v75 Biochemical and structural insights into how amino acids regulate pyruvate kinase muscle isoform 2.
Resolution2.85 Å
Binding residue
(original residue number in PDB)		K270 E272 A293 G295 D296 T328
Binding residue
(residue number reindexed from 1)		K256 E258 A279 G281 D282 T314
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) R73 R120 K270 T328
Catalytic site (residue number reindexed from 1) R59 R106 K256 T314
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.
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:6v75, PDBe:6v75, PDBj:6v75
PDBsum6v75
PubMed32144209
UniProtP14618|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

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