Structure of PDB 1dr7 Chain A

Receptor sequence
>1dr7A (length=186) Species: 9031 (Gallus gallus) [Search protein sequence]
VRSLNSIVAVCQNMGIGKDGNLPWPPLRNEYKYFQRMTSTSHVEGKQNAV
IMGKKTWFSIPEKNRPLKDRINIVLSRELKEAPKGAHYLSKSLDDALALL
DSPELKSKVDMVWIVGGTAVYKAAMEKPINHRLFVTRILHEFESDTFFPE
IDYKDFKLLTEYPGVPADIQEEDGIQYKFEVYQKSV
3D structure
PDB1dr7 Primary Structure of Chicken Liver Dihydrofolate Reductase
ChainA
Resolution2.4 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 NAP A V8 A9 I16 G20 N21 L22 G53 K54 K55 T56 L75 S76 R77 E78 K91 V115 G117 A119 V8 A9 I16 G20 N21 L22 G53 K54 K55 T56 L75 S76 R77 E78 K91 V115 G117 A119
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:1dr7, PDBe:1dr7, PDBj:1dr7
PDBsum1dr7
PubMed
UniProtP00378|DYR_CHICK Dihydrofolate reductase (Gene Name=DHFR)

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