Structure of PDB 1ex8 Chain A Binding Site BS01

Receptor Information
>1ex8 Chain A (length=158) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TVAYIAIGSNLASPLEQVNAALKALGDIPESHILTVSSFYRTPPLGPQDQ
PDYLNAAVALETSLAPEELLNHTQRIELQQGRVRKAERWGPRTLDLDIML
FGNEVINTERLTVPHYDMKNRGFMLWPLFEIAPELVFPDGEMLRQILHTR
AFDKLNKW
Ligand information
Ligand IDA4P
InChIInChI=1S/C17H24N10O17P4/c18-12-8-14(22-4-21-12)27(5-23-8)16-11(29)10(28)7(41-16)3-40-46(33,34)43-48(37,38)44-47(35,36)42-45(31,32)39-2-6-1-20-13-9(24-6)15(30)26-17(19)25-13/h4-5,7,10-11,16,28-29H,1-3H2,(H,31,32)(H,33,34)(H,35,36)(H,37,38)(H2,18,21,22)(H4,19,20,25,26,30)/t7-,10-,11-,16-/m1/s1
InChIKeyZKRKFZJAQKKHKL-SUGPNEFASA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@@](=O)(O)O[P@@](=O)(O)O[P@@](=O)(O)O[P@@](=O)(O)OCC4=NC5=C(NC4)N=C(NC5=O)N)O)O)N
ACDLabs 10.04O=C2NC(=NC=1NCC(=NC=12)COP(=O)(O)OP(=O)(O)OP(=O)(O)OP(=O)(O)OCC5OC(n4cnc3c(ncnc34)N)C(O)C5O)N
CACTVS 3.341NC1=NC2=C(N=C(CN2)CO[P](O)(=O)O[P](O)(=O)O[P](O)(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O)[CH]3O)n4cnc5c(N)ncnc45)C(=O)N1
CACTVS 3.341NC1=NC2=C(N=C(CN2)CO[P@@](O)(=O)O[P@@](O)(=O)O[P@@](O)(=O)O[P@@](O)(=O)OC[C@H]3O[C@H]([C@H](O)[C@@H]3O)n4cnc5c(N)ncnc45)C(=O)N1
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)OP(=O)(O)OCC4=NC5=C(NC4)N=C(NC5=O)N)O)O)N
FormulaC17 H24 N10 O17 P4
Name6-(ADENOSINE TETRAPHOSPHATE-METHYL)-7,8-DIHYDROPTERIN
ChEMBL
DrugBankDB04158
ZINCZINC000098208626
PDB chain1ex8 Chain A Residue 171 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1ex8 Bisubstrate analogue inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase: synthesis and biochemical and crystallographic studies.
Resolution1.85 Å
Binding residue
(original residue number in PDB)		T42 P43 L45 Y53 N55 Q74 R82 R84 R88 W89 R92 D97 I98 R110 L111 T112 H115 F123
Binding residue
(residue number reindexed from 1)		T42 P43 L45 Y53 N55 Q74 R82 R84 R88 W89 R92 D97 I98 R110 L111 T112 H115 F123
Annotation score3
Binding affinityMOAD: Kd=0.47uM
PDBbind-CN: -logKd/Ki=6.33,Kd=0.47uM
Enzymatic activity
Catalytic site (original residue number in PDB) R82 R92 D95 D97
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1ex8, PDBe:1ex8, PDBj:1ex8
PDBsum1ex8
PubMed11311059
UniProtP26281|HPPK_ECOLI 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (Gene Name=folK)

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