Structure of PDB 1tmm Chain B Binding Site BS04

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 information
Ligand IDHHR
InChIInChI=1S/C7H7N5O2/c8-7-11-5-4(6(14)12-7)10-3(2-13)1-9-5/h1,13H,2H2,(H3,8,9,11,12,14)
InChIKeyXGWIBNWDLMIPNF-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1c(nc2c(n1)N=C(NC2=O)N)CO
ACDLabs 10.04O=C1c2nc(cnc2N=C(N1)N)CO
CACTVS 3.341NC1=Nc2ncc(CO)nc2C(=O)N1
FormulaC7 H7 N5 O2
Name6-HYDROXYMETHYLPTERIN
ChEMBLCHEMBL101541
DrugBankDB03197
ZINCZINC000016051887
PDB chain1tmm Chain B Residue 381 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1tmm 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.
Resolution1.25 Å
Binding residue
(original residue number in PDB)		T242 P243 L245 Y253 N255 R292 D295 F323
Binding residue
(residue number reindexed from 1)		T42 P43 L45 Y53 N55 R92 D95 F123
Annotation score1
Binding affinityMOAD: Kd=1.1uM
Enzymatic activity
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.
Gene Ontology
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1tmm, PDBe:1tmm, PDBj:1tmm
PDBsum1tmm
PubMed15952765
UniProtP26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)

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