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Receptor Information

>1tmm Chain B (length=158) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQ
PDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERAGPRTLDLDIML
FGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTR
AFDKLNKW

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

1tmm Chain B Residue 371 [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	1tmm Is the Critical Role of Loop 3 of Escherichia coli 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase in Catalysis Due to Loop-3 Residues Arginine-84 and Tryptophan-89? Site-Directed Mutagenesis, Biochemical, and Crystallographic Studies.
Resolution	1.25 Å
Binding residue (original residue number in PDB)	L270 Q274 R282 K285 A286 R292 D295 D297 I298 R310 L311 T312 H315 Y316 R321
Binding residue (residue number reindexed from 1)	L70 Q74 R82 K85 A86 R92 D95 D97 I98 R110 L111 T112 H115 Y116 R121
Annotation score	3
Binding affinity	MOAD: Kd=0.23uM

Catalytic site (original residue number in PDB)	R282 R292 D295 D297
Catalytic site (residue number reindexed from 1)	R82 R92 D95 D97
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:1tmm, PDBe:1tmm, PDBj:1tmm
PDBsum	1tmm
PubMed	15952765
UniProt	P26281\|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)

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Structure of PDB 1tmm Chain B Binding Site BS03