Structure of PDB 3fl9 Chain B

Receptor sequence
>3fl9B (length=158) Species: 1392 (Bacillus anthracis) [Search protein sequence]
MIVSFMVAMDENRVIGKDNLPWRLPSELQYVKKTTMGHPLIMGRKNYEAI
GRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCKNEEEIFIFGGAQI
YDLFLPYVDKLYITKIHHAFEGDTFFPEMDWKEVFVEKGLTDEKNPYTYY
YHVYEKQQ
3D structure
PDB3fl9 Crystal structure of Bacillus anthracis dihydrofolate reductase with the dihydrophthalazine-based trimethoprim derivative RAB1 provides a structural explanation of potency and selectivity.
ChainB
Resolution2.4 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 L20 W22 E27 L28 V31 L54 I92 T114
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 B Y108 D110 Y107 D109
BS02 TOP B M6 V7 A8 L21 E28 V32 A50 I51 F96 M6 V7 A8 L20 E27 V31 A49 I50 F95 MOAD: ic50=77.2mM
BindingDB: Ki=24100nM,IC50=71000nM
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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Cellular Component
External links
PDB RCSB:3fl9, PDBe:3fl9, PDBj:3fl9
PDBsum3fl9
PubMed19364848
UniProtQ81R22

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