Structure of PDB 4dfr Chain A

Receptor sequence

>4dfrA (length=159) Species: 37762 (Escherichia coli B)

MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLDKPVIMGRHTWESI
GRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVY
EQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHS
YCFKILERR

3D structure

• PDB: 4dfr Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.
• Chain: A
• Resolution: 1.7 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): I5 M20 W22 D27 L28 F31 L54 I91 T113
• Catalytic site (residue number reindexed from 1): I5 M20 W22 D27 L28 F31 L54 I91 T113
• 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	MTX	A	I5 A6 D27 F31 K32 I50 R52 L54 R57 I94	I5 A6 D27 F31 K32 I50 R52 L54 R57 I94	BindingDB: IC50=8.8nM,EC50=1nM

Gene Ontology

Molecular Function

• GO:0004146 dihydrofolate reductase activity
• GO:0005515 protein binding
• GO:0005542 folic acid binding
• GO:0016491 oxidoreductase activity
• GO:0050661 NADP binding
• GO:0051870 methotrexate binding
• GO:0051871 dihydrofolic acid binding
• GO:0070401 NADP+ binding
• GO:0070402 NADPH binding

Biological Process

• GO:0006730 one-carbon metabolic process
• GO:0009257 10-formyltetrahydrofolate biosynthetic process
• GO:0009410 response to xenobiotic stimulus
• GO:0031427 response to methotrexate
• GO:0046452 dihydrofolate metabolic process
• GO:0046654 tetrahydrofolate biosynthetic process
• GO:0046655 folic acid metabolic process
• GO:0046656 folic acid biosynthetic process
• GO:0046677 response to antibiotic

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:4dfr, PDBe:4dfr, PDBj:4dfr
• PDBsum: 4dfr
• PubMed: 6815178
• UniProt: P0ABQ4|DYR_ECOLI Dihydrofolate reductase (Gene Name=folA)