Structure of PDB 1dr3 Chain A

Receptor sequence
>1dr3A (length=186) Species: 9031 (Gallus gallus) [Search protein sequence]
VRSLNSIVAVCQNMGIGKDGNLPWPPLRNEYKYFQRMTSTSHVEGKQNAV
IMGKKTWFSIPEKNRPLKDRINIVLSRELKEAPKGAHYLSKSLDDALALL
DSPELKSKVDMVWIVGGTAVYKAAMEKPINHRLFVTRILHEFESDTFFPE
IDYKDFKLLTEYPGVPADIQEEDGIQYKFEVYQKSV
3D structure
PDB1dr3 Crystal structures of chicken liver dihydrofolate reductase: binary thioNADP+ and ternary thioNADP+.biopterin complexes.
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 V8 A9 I16 G20 N21 L22 G53 K54 K55 T56 L75 S76 R77 E78 K91 V115 G117 V120 T146 V8 A9 I16 G20 N21 L22 G53 K54 K55 T56 L75 S76 R77 E78 K91 V115 G117 V120 T146
BS02 HBI A I7 E30 F34 V115 I7 E30 F34 V115
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

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1dr3, PDBe:1dr3, PDBj:1dr3
PDBsum1dr3
PubMed8334118
UniProtP00378|DYR_CHICK Dihydrofolate reductase (Gene Name=DHFR)

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