Structure of PDB 1hfq Chain A Binding Site BS02
Receptor Information
>1hfq Chain A (length=186) Species:
9606
(Homo sapiens) [
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VGSLNCIVAVSQNMGIGKNGDLPWPPLRNESRYFQRMTTTSSVEGKQNLV
IMGKKTWFSIPEKNRPLKGRINLVLSRELKEPPQGAHFLSRSLDDALKLT
EQPELANKVDMVWIVGGSSVYKEAMNHPGHLKLFVTRIMQDFESDTFFPE
IDLEKYKLLPEYPGVLSDVQEEKGIKYKFEVYEKND
Ligand information
Ligand ID
MOT
InChI
InChI=1S/C20H22N6O6/c1-26(8-11-9-32-18-15(11)16(21)24-20(22)25-18)12-4-2-10(3-5-12)17(29)23-13(19(30)31)6-7-14(27)28/h2-5,9,13H,6-8H2,1H3,(H,23,29)(H,27,28)(H,30,31)(H4,21,22,24,25)/t13-/m0/s1
InChIKey
WXINNGCGSCFUCR-ZDUSSCGKSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=C(O)C(NC(=O)c1ccc(cc1)N(C)Cc2c3c(nc(nc3oc2)N)N)CCC(=O)O
OpenEye OEToolkits 1.5.0
C[N@](Cc1coc2c1c(nc(n2)N)N)c3ccc(cc3)C(=O)N[C@@H](CCC(=O)O)C(=O)O
CACTVS 3.341
CN(Cc1coc2nc(N)nc(N)c12)c3ccc(cc3)C(=O)N[CH](CCC(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0
CN(Cc1coc2c1c(nc(n2)N)N)c3ccc(cc3)C(=O)NC(CCC(=O)O)C(=O)O
CACTVS 3.341
CN(Cc1coc2nc(N)nc(N)c12)c3ccc(cc3)C(=O)N[C@@H](CCC(O)=O)C(O)=O
Formula
C20 H22 N6 O6
Name
N-[4-[(2,4-DIAMINOFURO[2,3D]PYRIMIDIN-5-YL)METHYL]METHYLAMINO]-BENZOYL]-L-GLUTAMATE
ChEMBL
CHEMBL104829
DrugBank
DB02026
ZINC
PDB chain
1hfq Chain A Residue 188 [
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Receptor-Ligand Complex Structure
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PDB
1hfq
Comparison of ternary crystal complexes of F31 variants of human dihydrofolate reductase with NADPH and a classical antitumor furopyrimidine.
Resolution
2.1 Å
Binding residue
(original residue number in PDB)
I7 V8 E30 F34 Q35 I60 N64 L67 R70
Binding residue
(residue number reindexed from 1)
I7 V8 E30 F34 Q35 I60 N64 L67 R70
Annotation score
2
Binding affinity
MOAD
: Ki=2.7nM
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
View graph for
Cellular Component
External links
PDB
RCSB:1hfq
,
PDBe:1hfq
,
PDBj:1hfq
PDBsum
1hfq
PubMed
9627670
UniProt
P00374
|DYR_HUMAN Dihydrofolate reductase (Gene Name=DHFR)
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