Structure of PDB 6ech Chain D Binding Site BS01

Receptor Information

>6ech Chain D (length=527) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

QELGTAFFQQQQLPAAMADTFLEHLCLLDIDSQPVAARSTSIIATIGPAS
RSVDRLKEMIKAGMNIARLNFSHGSHEYHAESIANIREATESFATSPLSY
RPVAIALDTKGPEIRTGVLQGGPESEVEIVKGSQVLVTVDPKFQTRGDAK
TVWVDYHNITRVVAVGGRIYIDDGLISLVVQKIGPEGLVTEVEHGGILGS
RKGVNLPNTEVDLPGLSEQDLLDLRFGVQHNVDIIFASFVRKASDVLAVR
DALGPEGQNIKIISKIENHEGVKKFDEILEVSDGIMVARGDLGIEIPAEK
VFLAQKMMIGRCNLAGKPVVCATQMLESMITKARPTRAETSDVANAVLDG
ADCIMLSGETAKGSFPVEAVMMQHAIAREAEAAVYHRQLFEELRRAAPLS
RDPTEVTAIGAVEASFKCCAAAIIVLTKTGRSAQLLSQYRPRAAVIAVTR
SAQAARQVHLSRGVFPLLYREPPEAIWADDVDRRVQFGIESGKLRGFLRV
GDLVIVVTGWRPGSGYTNIMRVLSVSH

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

6ech Chain D Residue 601 [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	6ech Distinct Hepatic PKA and CDK Signaling Pathways Control Activity-Independent Pyruvate Kinase Phosphorylation and Hepatic Glucose Production.
Resolution	2.19 Å
Binding residue (original residue number in PDB)	L443 T444 K445 T446 S449 R501 G526 R528 P529 G530 S531 Y533 T534
Binding residue (residue number reindexed from 1)	L426 T427 K428 T429 S432 R484 G509 R511 P512 G513 S514 Y516 T517
Annotation score	1

Enzymatic activity

Catalytic site (original residue number in PDB)	R85 R132 K282 T340
Catalytic site (residue number reindexed from 1)	R68 R115 K265 T323
Enzyme Commision number	2.7.1.40: pyruvate kinase.

Gene Ontology

	Molecular Function
GO:0000287	magnesium ion binding
GO:0003824	catalytic activity
GO:0004743	pyruvate kinase activity
GO:0005524	ATP binding
GO:0016301	kinase activity
GO:0030955	potassium ion binding
GO:0046872	metal ion binding
GO:0048029	monosaccharide binding

	Biological Process
GO:0001666	response to hypoxia
GO:0006096	glycolytic process
GO:0007584	response to nutrient
GO:0009749	response to glucose
GO:0010038	response to metal ion
GO:0016310	phosphorylation
GO:0032869	cellular response to insulin stimulus
GO:0033198	response to ATP
GO:0042866	pyruvate biosynthetic process
GO:0051591	response to cAMP
GO:0051707	response to other organism
GO:0071872	cellular response to epinephrine stimulus

	Cellular Component
GO:0005737	cytoplasm
GO:0005829	cytosol
GO:0005886	plasma membrane

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Molecular Function

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Biological Process

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Cellular Component

External links

PDB	RCSB:6ech, PDBe:6ech, PDBj:6ech
PDBsum	6ech
PubMed	31825824
UniProt	P12928\|KPYR_RAT Pyruvate kinase PKLR (Gene Name=Pklr)

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