Structure of PDB 3fre Chain X Binding Site BS02

Receptor Information
>3fre Chain X (length=157) Species: 1280 (Staphylococcus aureus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
TLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESI
GKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEE
MIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHT
FLHLIRK
Ligand information
Ligand IDTOP
InChIInChI=1S/C14H18N4O3/c1-19-10-5-8(6-11(20-2)12(10)21-3)4-9-7-17-14(16)18-13(9)15/h5-7H,4H2,1-3H3,(H4,15,16,17,18)
InChIKeyIEDVJHCEMCRBQM-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341COc1cc(Cc2cnc(N)nc2N)cc(OC)c1OC
OpenEye OEToolkits 1.5.0COc1cc(cc(c1OC)OC)Cc2cnc(nc2N)N
ACDLabs 10.04n1c(N)c(cnc1N)Cc2cc(OC)c(OC)c(OC)c2
FormulaC14 H18 N4 O3
NameTRIMETHOPRIM
ChEMBLCHEMBL22
DrugBankDB00440
ZINCZINC000006627681
PDB chain3fre Chain X Residue 300 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3fre Increased hydrophobic interactions of iclaprim with Staphylococcus aureus dihydrofolate reductase are responsible for the increase in affinity and antibacterial activity
Resolution2.2 Å
Binding residue
(original residue number in PDB)		L5 V6 A7 D27 L28 V31 F92
Binding residue
(residue number reindexed from 1)		L5 V6 A7 D27 L28 V31 F92
Annotation score1
Binding affinityMOAD: Ki=0.0006uM
BindingDB: Ki=3.4nM,IC50=14.4nM
Enzymatic activity
Catalytic site (original residue number in PDB) L5
Catalytic site (residue number reindexed from 1) L5
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3fre, PDBe:3fre, PDBj:3fre
PDBsum3fre
PubMed19211577
UniProtP0A017|DYR_STAAU Dihydrofolate reductase (Gene Name=folA)

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