Structure of PDB 1dr2 Chain A

Receptor sequence

>1dr2A (length=186) Species: 9031 (Gallus gallus)

VRSLNSIVAVCQNMGIGKDGNLPWPPLRNEYKYFQRMTSTSHVEGKQNAV
IMGKKTWFSIPEKNRPLKDRINIVLSRELKEAPKGAHYLSKSLDDALALL
DSPELKSKVDMVWIVGGTAVYKAAMEKPINHRLFVTRILHEFESDTFFPE
IDYKDFKLLTEYPGVPADIQEEDGIQYKFEVYQKSV

3D structure

• PDB: 1dr2 Crystal structures of chicken liver dihydrofolate reductase: binary thioNADP+ and ternary thioNADP+.biopterin complexes.
• Chain: A
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): L22 W24 E30 Y31 F34 L67 W113 T136
• Catalytic site (residue number reindexed from 1): L22 W24 E30 Y31 F34 L67 W113 T136
• 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	TAP	A	A9 I16 G20 N21 G53 K54 K55 T56 L75 S76 R77 E78 K91 V115 G117 A119 V120 T146	A9 I16 G20 N21 G53 K54 K55 T56 L75 S76 R77 E78 K91 V115 G117 A119 V120 T146

Gene Ontology

Molecular Function

• GO:0003723 RNA binding
• GO:0003729 mRNA binding
• GO:0004146 dihydrofolate reductase activity
• GO:0016491 oxidoreductase activity
• GO:0050661 NADP binding

Biological Process

• GO:0006730 one-carbon metabolic process
• GO:0031427 response to methotrexate
• GO:0046452 dihydrofolate metabolic process
• GO:0046653 tetrahydrofolate metabolic process
• GO:0046654 tetrahydrofolate biosynthetic process
• GO:0046655 folic acid metabolic process

Cellular Component

• GO:0005739 mitochondrion

External links

• PDB: RCSB:1dr2, PDBe:1dr2, PDBj:1dr2
• PDBsum: 1dr2
• PubMed: 8334118
• UniProt: P00378|DYR_CHICK Dihydrofolate reductase (Gene Name=DHFR)