Structure of PDB 1dyr Chain A Binding Site BS02

Receptor Information
>1dyr Chain A (length=205) Species: 4754 (Pneumocystis carinii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFES
MNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDHA
LELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDIH
CDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFEM
WTRDL
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 chain1dyr Chain A Residue 407 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1dyr The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution.
Resolution1.86 Å
Binding residue
(original residue number in PDB)		I10 L25 E32 F36 I123
Binding residue
(residue number reindexed from 1)		I9 L24 E31 F35 I122
Annotation score1
Binding affinityMOAD: ic50=20uM
BindingDB: IC50=12000nM,Ki=280000nM
Enzymatic activity
Catalytic site (original residue number in PDB) L25 E32
Catalytic site (residue number reindexed from 1) L24 E31
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:0005739 mitochondrion

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dyr, PDBe:1dyr, PDBj:1dyr
PDBsum1dyr
PubMed7866743
UniProtP16184|DYR_PNECA Dihydrofolate reductase

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