Structure of PDB 6ttq Chain C Binding Site BS02

Receptor Information

>6ttq Chain C (length=510) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

MADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNV
ARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRT
GLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVG
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

PDB chain

6ttq Chain C Residue 1002 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	6ttq Fragment-based drug discovery using cryo-EM.
Resolution	2.7 Å
Binding residue (original residue number in PDB)	T432 S434 S437 R489 G514 R516 G518 S519 F521
Binding residue (residue number reindexed from 1)	T411 S413 S416 R468 G493 R495 G497 S498 F500
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	R73 R120 K270 T328
Catalytic site (residue number reindexed from 1)	R52 R99 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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Cellular Component

External links

PDB	RCSB:6ttq, PDBe:6ttq, PDBj:6ttq
PDBsum	6ttq
PubMed	31877353
UniProt	P14618\|KPYM_HUMAN Pyruvate kinase PKM (Gene Name=PKM)

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