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Structure of PDB 6wp5 Chain B Binding Site BS03

Receptor Information >6wp5 Chain B (length=510) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure] AMADTFLEHMCRLDIDDPPITARNTGIICTIGPASRSVETLKEMIKSGMN VARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIR TGLIKGSGAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVG SKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAV SEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKI ENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRAG KPVICATQMLESMIKKPRPTRAEGSDVANAVLDGADCIMLSGETAKGDYP LEAVRMQHLIAREAEAAIYHLQLFEELRRLAPITSDPTEATAVGAVEASF KCCSGAIIVLTKSGRSAHQVARYRPRAPIIAVTRNPQTARQAHLYRGIFP VLCKDPVQEAWAEDVDLRVNFAMNVGKARGFFKKGDVVIVLTGWRPGSGF TNTMRVVPVP

Ligand information Ligand ID FBP InChI InChI=1S/C6H14O12P2/c7-4-3(1-16-19(10,11)12)18-6(9,5(4)8)2-17-20(13,14)15/h3-5,7-9H,1-2H2,(H2,10,11,12)(H2,13,14,15)/t3-,4-,5+,6-/m1/s1 InChIKey RNBGYGVWRKECFJ-ARQDHWQXSA-N SMILES Software SMILES CACTVS 3.341 O[C@H]1[C@H](O)[C@@](O)(CO[P](O)(O)=O)O[C@@H]1CO[P](O)(O)=O CACTVS 3.341 O[CH]1[CH](O)[C](O)(CO[P](O)(O)=O)O[CH]1CO[P](O)(O)=O ACDLabs 10.04 O=P(O)(O)OCC1OC(O)(COP(=O)(O)O)C(O)C1O OpenEye OEToolkits 1.5.0 C(C1C(C(C(O1)(COP(=O)(O)O)O)O)O)OP(=O)(O)O OpenEye OEToolkits 1.5.0 C([C@@H]1[C@H]([C@@H]([C@](O1)(COP(=O)(O)O)O)O)O)OP(=O)(O)O Formula C6 H14 O12 P2 Name 1,6-di-O-phosphono-beta-D-fructofuranose; BETA-FRUCTOSE-1,6-DIPHOSPHATE; FRUCTOSE-1,6-BISPHOSPHATE; 1,6-di-O-phosphono-beta-D-fructose; 1,6-di-O-phosphono-D-fructose; 1,6-di-O-phosphono-fructose ChEMBL CHEMBL97893 DrugBank DB04551 ZINC ZINC000004096694 PDB chain 6wp5 Chain B Residue 607 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure Global view Local view Structure summary [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] [Spin on] [Spin off] [Reset] [High quality] [Low quality] [White background] [Black background] PDB 6wp5 Structural basis for allosteric regulation of pyruvate kinase M2 by phosphorylation and acetylation. Resolution 2.17 Å Binding residue (original residue number in PDB) T432 S434 S437 S519 G520 Binding residue (residue number reindexed from 1) T411 S413 S416 S498 G499 Annotation score 1 Binding affinity MOAD: Kd=1uM

Enzymatic activity Catalytic site (original residue number in PDB) R73 R120 K270 T328 Catalytic site (residue number reindexed from 1) R53 R100 K249 T307 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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