Structure of PDB 1dra Chain B

Receptor sequence

>1draB (length=159) Species: 562 (Escherichia coli)

MISLIAALAVDRVIGMENAMPWNLPAELAWFKRNTLDKPVIMGRHTWESI
GRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVY
EQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHS
YCFEILERR

3D structure

• PDB: 1dra Crystal structure of unliganded Escherichia coli dihydrofolate reductase. Ligand-induced conformational changes and cooperativity in binding.
• Chain: B
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): I5 M20 W22 E27 L28 F31 L54 I91 T113
• Catalytic site (residue number reindexed from 1): I5 M20 W22 E27 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	B	I5 A6 A7 E27 L28 F31 K32 I50 R52 R57 I94	I5 A6 A7 E27 L28 F31 K32 I50 R52 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:1dra, PDBe:1dra, PDBj:1dra
• PDBsum: 1dra
• PubMed: 1998681
• UniProt: P0ABQ4|DYR_ECOLI Dihydrofolate reductase (Gene Name=folA)