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Receptor Information

>1ru1 Chain A (length=143) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPPDYLNA
AVALETSLAPEELLNHTQRIELQQGRRTLDLDIMLFGNEVINTERLTVPH
YDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTRAFDKLNKW

Ligand ID

APC

InChI

InChI=1S/C11H18N5O12P3/c12-9-6-10(14-2-13-9)16(3-15-6)11-8(18)7(17)5(27-11)1-26-29(19,20)4-30(21,22)28-31(23,24)25/h2-3,5,7-8,11,17-18H,1,4H2,(H,19,20)(H,21,22)(H2,12,13,14)(H2,23,24,25)/t5-,7-,8-,11-/m1/s1

InChIKey

CAWZRIXWFRFUQB-IOSLPCCCSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(C[P@](=O)(O)OP(=O)(O)O)O)O)O)N
CACTVS 3.341	Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)C[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0	c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(CP(=O)(O)OP(=O)(O)O)O)O)O)N
ACDLabs 10.04	O=P(O)(O)OP(=O)(O)CP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341	Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)C[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O

Formula

C11 H18 N5 O12 P3

Name

DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER;
ALPHA,BETA-METHYLENEADENOSINE-5'-TRIPHOSPHATE

PDB chain

1ru1 Chain A Residue 171 [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	1ru1 Essential Roles of a Dynamic Loop in the Catalysis of 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase.
Resolution	1.4 Å
Binding residue (original residue number in PDB)	Q74 D95 D97 I98 R110 L111 T112 H115 Y116 R121
Binding residue (residue number reindexed from 1)	Q68 D80 D82 I83 R95 L96 T97 H100 Y101 R106
Annotation score	3
Binding affinity	PDBbind-CN: -logKd/Ki=4.74,Kd=18uM

Catalytic site (original residue number in PDB)	R92 D95 D97
Catalytic site (residue number reindexed from 1)	R77 D80 D82
Enzyme Commision number	2.7.6.3: 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.

	Molecular Function
GO:0000287	magnesium ion binding
GO:0003848	2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity
GO:0005524	ATP binding
GO:0016301	kinase activity

	Biological Process
GO:0009396	folic acid-containing compound biosynthetic process
GO:0016310	phosphorylation
GO:0046654	tetrahydrofolate biosynthetic process
GO:0046656	folic acid biosynthetic process

PDB	RCSB:1ru1, PDBe:1ru1, PDBj:1ru1
PDBsum	1ru1
PubMed	14769023
UniProt	P26281\|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)

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Structure of PDB 1ru1 Chain A Binding Site BS03