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Receptor Information

>1k6m Chain B (length=432) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

NSPTMVIMVGLPARGKTYISTKLTRYLNFIGTPTKVFNLGQYRREAVSYK
NYEFFLPDNMEALQIRKQCALAALKDVHNYLSHEEGHVAVFDATNTTRER
RSLILQFAKEHGYKVFFIESICNDPGIIAENIRQVKLGSPDYIDCDREKV
LEDFLKRIECYEVNYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHIQSR
TVYYLMNIHVTPRSIYLCRHGESELNIRGRIGGDSGLSVRGKQYAYALAN
FIQSQGISSLKVFTSRMKRTIQTAEALGVPYEQFKALNEIDAGVCEEMTY
EEIQEHYPEEFALRDQDKYRYRYPKGESYEDLVQRLEPVIMELERQENVL
VICHQAVMRCLLAYFLDKSSEELPYLKCPLHTVLKLTPVAYGCKVESIYL
NVEAVNTHREKPENVDITREPEEALDTVPAHY

Ligand ID

AGS

InChI

InChI=1S/C10H16N5O12P3S/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(25-10)1-24-28(18,19)26-29(20,21)27-30(22,23)31/h2-4,6-7,10,16-17H,1H2,(H,18,19)(H,20,21)(H2,11,12,13)(H2,22,23,31)/t4-,6-,7-,10-/m1/s1

InChIKey

NLTUCYMLOPLUHL-KQYNXXCUSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.7.6	c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=S)(O)O)O)O)N
CACTVS 3.370	Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=S)[C@@H](O)[C@H]3O
CACTVS 3.370	Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(=O)O[P](O)(O)=S)[CH](O)[CH]3O
OpenEye OEToolkits 1.7.6	c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)COP(=O)(O)OP(=O)(O)OP(=S)(O)O)O)O)N
ACDLabs 12.01	O=P(O)(OP(=S)(O)O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O

Formula

C10 H16 N5 O12 P3 S

Name

PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER;
ATP-GAMMA-S;
ADENOSINE 5'-(3-THIOTRIPHOSPHATE);
ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE);
ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE

PDB chain

1k6m Chain B Residue 503 [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	1k6m Tissue-specific structure/function differentiation of the liver isoform of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase.
Resolution	2.4 Å
Binding residue (original residue number in PDB)	A51 R52 G53 K54 T55 Y56 D130 S158 N169 Q172 V173 K174 V222 Y429
Binding residue (residue number reindexed from 1)	A13 R14 G15 K16 T17 Y18 D92 S120 N131 Q134 V135 K136 V184 Y391
Annotation score	4

Catalytic site (original residue number in PDB)	R257 H258 N264 R307 E327 H392
Catalytic site (residue number reindexed from 1)	R219 H220 N226 R269 E289 H354
Enzyme Commision number	2.7.1.105: 6-phosphofructo-2-kinase. 3.1.3.46: fructose-2,6-bisphosphate 2-phosphatase.

	Molecular Function
GO:0003824	catalytic activity
GO:0003873	6-phosphofructo-2-kinase activity
GO:0004331	fructose-2,6-bisphosphate 2-phosphatase activity
GO:0005515	protein binding
GO:0005524	ATP binding
GO:0016301	kinase activity
GO:0016787	hydrolase activity
GO:0019900	kinase binding
GO:0042802	identical protein binding
GO:0070095	fructose-6-phosphate binding

	Biological Process
GO:0006000	fructose metabolic process
GO:0006003	fructose 2,6-bisphosphate metabolic process
GO:0006094	gluconeogenesis
GO:0006096	glycolytic process
GO:0016310	phosphorylation
GO:0031100	animal organ regeneration
GO:0032868	response to insulin
GO:0033762	response to glucagon
GO:0042594	response to starvation
GO:0046835	carbohydrate phosphorylation
GO:0051384	response to glucocorticoid
GO:0051591	response to cAMP
GO:1904539	negative regulation of glycolytic process through fructose-6-phosphate
GO:1904540	positive regulation of glycolytic process through fructose-6-phosphate

	Cellular Component
GO:0005829	cytosol
GO:0043540	6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex

PDB	RCSB:1k6m, PDBe:1k6m, PDBj:1k6m
PDBsum	1k6m
PubMed	12379646
UniProt	P16118\|F261_HUMAN 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 1 (Gene Name=PFKFB1)

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Structure of PDB 1k6m Chain B Binding Site BS01