Structure of PDB 5isq Chain X Binding Site BS02

Receptor Information
>5isq 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]
TLSILVAHDLQRVIGFENQLPWHLPNDLKNVKKLSTGHTLVMGRKTFESI
GKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLYEE
MIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHT
FLHLIRK
Ligand information
Ligand IDU06
InChIInChI=1S/C23H22N4O3/c1-3-19-18(21(24)27-23(25)26-19)6-4-5-17-13-16(11-12-20(17)30-2)14-7-9-15(10-8-14)22(28)29/h7-13H,3,5H2,1-2H3,(H,28,29)(H4,24,25,26,27)
InChIKeyKQGRJTMRAQWNLV-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.4CCc1c(c(nc(n1)N)N)C#CCc2cc(ccc2OC)c3ccc(cc3)C(=O)O
CACTVS 3.385CCc1nc(N)nc(N)c1C#CCc2cc(ccc2OC)c3ccc(cc3)C(O)=O
FormulaC23 H22 N4 O3
Name4-[3-[3-[2,4-bis(azanyl)-6-ethyl-pyrimidin-5-yl]prop-2-ynyl]-4-methoxy-phenyl]benzoic acid;
3'-(3-(2,4-diamino-6-ethylpyrimidin-5-yl)prop-2-yn-1-yl)-4'-methoxy-[1,1'-biphenyl]-4-carboxylic acid;
UCP1106
ChEMBLCHEMBL3827532
DrugBank
ZINCZINC000584905708
PDB chain5isq Chain X Residue 202 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5isq Charged Propargyl-Linked Antifolates Reveal Mechanisms of Antifolate Resistance and Inhibit Trimethoprim-Resistant MRSA Strains Possessing Clinically Relevant Mutations.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		L5 V6 D27 L28 V31 S49 I50 F92
Binding residue
(residue number reindexed from 1)		L5 V6 D27 L28 V31 S49 I50 F92
Annotation score1
Binding affinityMOAD: Ki=158.3nM
BindingDB: Ki=4.8nM
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:5isq, PDBe:5isq, PDBj:5isq
PDBsum5isq
PubMed27308944
UniProtP0A017|DYR_STAAU Dihydrofolate reductase (Gene Name=folA)

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