Structure of PDB 3fl8 Chain A

Receptor sequence

>3fl8A (length=166) Species: 1392 (Bacillus anthracis)

MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEA
IGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCKNEEEIFIFGGAQ
IYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNP
YTYYYHVYEKQQLVPR

3D structure

• PDB: 3fl8 Crystal structure of Bacillus anthracis dihydrofolate reductase with the dihydrophthalazine-based trimethoprim derivative RAB1 provides a structural explanation of potency and selectivity.
• Chain: A
• Resolution: 2.2881 Å

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	A	Y108 D110	Y108 D110
BS02	RAR	A	M6 V7 A8 L21 E28 L29 V32 I51 L55 R58 F96	M6 V7 A8 L21 E28 L29 V32 I51 L55 R58 F96	MOAD: ic50=54nM PDBbind-CN: -logKd/Ki=7.27,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

External links

• PDB: RCSB:3fl8, PDBe:3fl8, PDBj:3fl8
• PDBsum: 3fl8
• PubMed: 19364848
• UniProt: Q81R22