Structure of PDB 2c2t Chain B Binding Site BS03

Receptor Information
>2c2t Chain B (length=186) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VGSLNCIVAVSQNMGIGKNGDLPWPPLRNEFRYFQRMTTTSSVEGKQNLV
IMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLT
EQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPE
IDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND
Ligand information
Ligand ID39B
InChIInChI=1S/C8H9B9N4/c1-3-4(5(18)21-6(19)20-3)2-8-7-9-11-10(8)14(8)12(7,8)13(7,9)15(9,11)16(10,11,14)17(12,13,14)15/h2H2,1H3,(H4,18,19,20,21)/q+1
InChIKeyLMKIHIJGTSLZFQ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 2.0.7B123B45B167B289B31B823B966B744B622[C@@]45[C+]321Cc1c(nc(nc1N)N)C
ACDLabs 10.04n1c(c(c(nc1N)N)CC29%12B8B%157%10B4[H]B53C2%11B36%13B45%15B67%14B89%10B%11%12%13%14)C
CACTVS 3.385Cc1nc(N)nc(N)c1C[C+]234[B-]56[B]78[B+]9%10[C]2%11[B]9%12%13[B]7%10%14[B]58%15[B]36%16[B]4%11%12[B]%13%14%15%16
CACTVS 3.385Cc1nc(N)nc(N)c1C[C+]234[B-]56[B]78[B+]9%10[C@@]2%11[B]9%12%13[B]7%10%14[B]58%15[B]36%16[B]4%11%12[B]%13%14%15%16
OpenEye OEToolkits 2.0.7B123B45B167B289B31B823B966B744B622C45[C+]321Cc1c(nc(nc1N)N)C
FormulaC8 H9 B9 N4
Name(S)-2,4-DIAMINO-5-((7,8-DICARBAUNDECABORAN-7-YL)METHYL)-6-METHYLPYRIMIDINE
ChEMBL
DrugBank
ZINC
PDB chain2c2t Chain B Residue 1189 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2c2t Novel Boron-Containing, Nonclassical Antifolates: Synthesis and Preliminary Biological and Structural Evaluation.
Resolution1.5 Å
Binding residue
(original residue number in PDB)		I7 V8 E30 F31 F34 I60
Binding residue
(residue number reindexed from 1)		I7 V8 E30 F31 F34 I60
Annotation score1
Binding affinityMOAD: ic50=15uM
Enzymatic activity
Catalytic site (original residue number in PDB) L22 E30
Catalytic site (residue number reindexed from 1) L22 E30
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
Gene Ontology
Molecular Function
GO:0000900 mRNA regulatory element binding translation repressor activity
GO:0003723 RNA binding
GO:0003729 mRNA binding
GO:0004146 dihydrofolate reductase activity
GO:0005542 folic acid binding
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
GO:0070402 NADPH binding
GO:1990825 sequence-specific mRNA binding
Biological Process
GO:0006729 tetrahydrobiopterin biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0017148 negative regulation of translation
GO:0031103 axon regeneration
GO:0031427 response to methotrexate
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:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005829 cytosol

View graph for
Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2c2t, PDBe:2c2t, PDBj:2c2t
PDBsum2c2t
PubMed17569517
UniProtP00374|DYR_HUMAN Dihydrofolate reductase (Gene Name=DHFR)

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