Structure of PDB 4eck Chain A

Receptor sequence
>4eckA (length=498) Species: 5811 (Toxoplasma gondii) [Search protein sequence]
KPVCLVVAMTPKRGIGINNGLPWPHLTTDFKHFSRVTKTTPEFNAVVMGR
KTWESMPRKFRPLVDRLNIVVSSSLKEEDIAAKEGQQRVRVCASLPAALS
LEEYKDSVDQIFVVGAGLYEAALSGVASHLYITRVAREFPCDVFFPAPGD
DILTYRPIFISKTFSDNGVPYDFVVLEKRSSAAAIAPVLAWMDEDRELIR
AVPHVHFRGHEEFQYLDLIADIINNGRTMDDRTGVGVISKFGCTMRYSLD
QAFPLLTTKRVFWKGVLEELLWFIRGDTNANHLSEKGVKIWDKNVTREFL
DSRNLPHREVGDIGPGYGFQWRHFGAAYKDMHTDYTGQGVDQLKNVIQML
RTNPTDRRMLMTAWNPAALDEMALPPCHLLCQFYVNDQKELSCIMYQRSC
DVGLGVPFNIASYSLLTLMVAHVCNLKPKEFIHFMGNTHVYTNHVEALKE
QLRREPRPFPIVNILNKERIKEIDDFTAEDFEVVGYVPHGRIQMEMAV
3D structure
PDB4eck First Three-Dimensional Structure of Toxoplasma gondii Thymidylate Synthase-Dihydrofolate Reductase: Insights for Catalysis, Interdomain Interactions, and Substrate Channeling.
ChainA
Resolution3.516 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L23 D31 E381 W403 Y429 C489 R510 D513
Catalytic site (residue number reindexed from 1) L21 D29 E269 W291 Y317 C377 R398 D401
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
2.1.1.45: thymidylate synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0004799 thymidylate synthase activity
GO:0008168 methyltransferase activity
GO:0016491 oxidoreductase activity
GO:0016741 transferase activity, transferring one-carbon groups
Biological Process
GO:0006231 dTMP biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0009165 nucleotide biosynthetic process
GO:0032259 methylation
GO:0046654 tetrahydrofolate biosynthetic process
Cellular Component
GO:0005739 mitochondrion
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4eck, PDBe:4eck, PDBj:4eck
PDBsum4eck
PubMed24053355
UniProtQ07422|DRTS_TOXGO Bifunctional dihydrofolate reductase-thymidylate synthase

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