User:Karan Hingorani/sandbox 1
From Proteopedia
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| - | E.coli DHFR is a small 159 amino acid protein approximately 18kDa. It has an a/b structure with eight central B strands and four helices. The protein can be thought to be made up of two subdomains, divided by the active site cleft. <scene name='User:Karan_Hingorani/sandbox_1/ | + | E.coli DHFR is a small 159 amino acid protein approximately 18kDa. It has an a/b structure with eight central B strands and four helices. The protein can be thought to be made up of two subdomains, divided by the active site cleft. The <scene name='User:Karan_Hingorani/sandbox_1/Adenosine_binding_loop/1'>Adenosine binding subdomain</scene> which consists of residues 38-88 and the major subdomain comprised of about 100 residues. Three loops can be found in the major subdomain and they make up about 50% of this domain. |
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===Catalysis=== | ===Catalysis=== | ||
Revision as of 16:29, 14 December 2011
Contents |
Introduction
Dihydrofolate Reductase (DHFR) is a crucial metabolic enzyme whose function is to reduce Dihydrofolate to Tetrahydrofolate, which can then be incorporated into the synthesis of Purines and amino acids. DHFR is classified as an oxidoreductase, which uses NADP+ as the electron acceptor (EC: 1.5.1.3). It is ubiquitously found and is now a popular target for anticancer drugs and antibiotics. free of any of its ligands is displayed here.
Structure
E.coli DHFR is a small 159 amino acid protein approximately 18kDa. It has an a/b structure with eight central B strands and four helices. The protein can be thought to be made up of two subdomains, divided by the active site cleft. The which consists of residues 38-88 and the major subdomain comprised of about 100 residues. Three loops can be found in the major subdomain and they make up about 50% of this domain.
Catalysis
Test
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Drug Target
metho and trimetho [1].
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PDB structures
2cbr - hCRABP I – human
1cbr - CRABP I + retinoic acid – mouse
