Structure of PDB 5noo Chain D

Receptor sequence
>5nooD (length=286) Species: 6239 (Caenorhabditis elegans) [Search protein sequence]
HLNQDEYKYLKQVEQILREGTRRDDTGTGTISIFGMQSKYCLRNGTIPLL
TTKRVYWKGVLEELLWFISGSTDGKLLMEKNVKIWEKNGDRAFLDNLGFT
SREEGDLGPVYGFQWRHFGAKYVDCHTDYSGQGVDQLAEVIRQIKEQPDS
RRIIMSAWNPSDLGQMVLPPCHTMCQFYVDNGELSCQLYQRSGDMGLGVP
FNLASYGLLTHMIAKVCGLKPGTLVHTLGDAHVYSNHVDALKIQLDREPY
AFPKIRFTRDVASIDDFTSDMIALDDYKCHPKIPMD
3D structure
PDB5noo Crystal structures of nematode (parasitic T. spiralis and free living C. elegans), compared to mammalian, thymidylate synthases (TS). Molecular docking and molecular dynamics simulations in search for nematode-specific inhibitors of TS.
ChainD
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E89 W111 Y137 C197 R217 D220
Catalytic site (residue number reindexed from 1) E63 W85 Y111 C171 R191 D194
Enzyme Commision number 2.1.1.45: thymidylate synthase.
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 UMP D C197 R217 S218 D220 G224 N228 H258 C171 R191 S192 D194 G198 N202 H232
BS02 D16 D R80 Y82 I110 D220 L223 G224 F227 Y260 R54 Y56 I84 D194 L197 G198 F201 Y234
Gene Ontology
Molecular Function
GO:0004799 thymidylate synthase activity
GO:0008168 methyltransferase activity
GO:0016741 transferase activity, transferring one-carbon groups
Biological Process
GO:0006231 dTMP biosynthetic process
GO:0006235 dTTP biosynthetic process
GO:0009165 nucleotide biosynthetic process
GO:0032259 methylation

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5noo, PDBe:5noo, PDBj:5noo
PDBsum5noo
PubMed28826032
UniProtQ9Y052

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