Structure of PDB 3fl8 Chain E

Receptor sequence
>3fl8E (length=166) Species: 1392 (Bacillus anthracis) [Search protein sequence]
MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEA
IGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCKNEEEIFIFGGAQ
IYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNP
YTYYYHVYEKQQLVPR
3D structure
PDB3fl8 Crystal structure of Bacillus anthracis dihydrofolate reductase with the dihydrophthalazine-based trimethoprim derivative RAB1 provides a structural explanation of potency and selectivity.
ChainE
Resolution2.2881 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M6 L21 W23 E28 L29 V32 L55 I93 T115
Catalytic site (residue number reindexed from 1) M6 L21 W23 E28 L29 V32 L55 I93 T115
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA E Y108 D110 Y108 D110
BS02 RAR E M6 V7 A8 L21 E28 L29 V32 K33 I51 L55 R58 F96 M6 V7 A8 L21 E28 L29 V32 K33 I51 L55 R58 F96 MOAD: ic50=54nM
BindingDB: IC50=54nM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
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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External links
PDB RCSB:3fl8, PDBe:3fl8, PDBj:3fl8
PDBsum3fl8
PubMed19364848
UniProtQ81R22

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