Structure of PDB 2fzj Chain A Binding Site BS02

Receptor Information
>2fzj Chain A (length=186) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VRPLNCIVAVSQNMGIGKNGDLPWPPLRNEFKYFQRMTTTSSVEGKQNLV
IMGRKTWFSIPEKNRPLKDRINIVLSRELKEPPRGAHFLAKSLDDALRLI
EQPELASKVDMVWIVGGSSVYQEAMNQPGHLRLFVTRIMQEFESDTFFPE
IDLGKYKLLPEYPGVLSEVQEEKGIKYKFEVYEKKD
Ligand information
Ligand IDDH3
InChIInChI=1S/C19H22N4O4/c1-26-15-10-12(9-14-11-22-19(21)23-18(14)20)8-13(17(15)27-2)6-4-3-5-7-16(24)25/h8,10-11H,3,5,7,9H2,1-2H3,(H,24,25)(H4,20,21,22,23)
InChIKeyJAGSWKLZBKKKJP-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341COc1cc(Cc2cnc(N)nc2N)cc(C#CCCCC(O)=O)c1OC
OpenEye OEToolkits 1.5.0COc1cc(cc(c1OC)C#CCCCC(=O)O)Cc2cnc(nc2N)N
ACDLabs 10.04O=C(O)CCCC#Cc1cc(cc(OC)c1OC)Cc2cnc(nc2N)N
FormulaC19 H22 N4 O4
Name2,4-DIAMINO-5-[3',4'-DIMETHOXY-5'-(5-CARBOXYL-1-PENTYNYL)]BENZYL PYRIMIDINE
ChEMBLCHEMBL300419
DrugBank
ZINCZINC000013646361
PDB chain2fzj Chain A Residue 188 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2fzj New insights into DHFR interactions: analysis of Pneumocystis carinii and mouse DHFR complexes with NADPH and two highly potent 5-(omega-carboxy(alkyloxy) trimethoprim derivatives reveals conformational correlations with activity and novel parallel ring stacking interactions.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		I7 V8 A9 L22 E30 F31 F34 Q35 S59 I60 K68 R70 V115
Binding residue
(residue number reindexed from 1)		I7 V8 A9 L22 E30 F31 F34 Q35 S59 I60 K68 R70 V115
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) L22 W24 E30 F31 F34 L67 M111 T136
Catalytic site (residue number reindexed from 1) L22 W24 E30 F31 F34 L67 M111 T136
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
Gene Ontology
Molecular Function
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
GO:0051871 dihydrofolic acid binding
Biological Process
GO:0006729 tetrahydrobiopterin biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0031103 axon regeneration
GO:0031427 response to methotrexate
GO:0035094 response to nicotine
GO:0035999 tetrahydrofolate interconversion
GO:0046452 dihydrofolate metabolic process
GO:0046653 tetrahydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
GO:0051000 positive regulation of nitric-oxide synthase activity
GO:2000121 regulation of removal of superoxide radicals
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005739 mitochondrion
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:2fzj, PDBe:2fzj, PDBj:2fzj
PDBsum2fzj
PubMed17019704
UniProtP00375|DYR_MOUSE Dihydrofolate reductase (Gene Name=Dhfr)

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