Structure of PDB 5ioq Chain D

Receptor sequence
>5ioqD (length=213) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MKIDILDKGFVELVDVMGNDLSAVRAARVSDEERDRHLIEYLMKHGHETP
FEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLSYEFYIPSPERL
EGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIVLPLNLYT
RFFWTVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCPWTFEAFL
KYAYKGDILKEVQ
3D structure
PDB5ioq Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase.
ChainD
Resolution1.93 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.148: thymidylate synthase (FAD).
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 FAD D T55 E58 I81 N163 R165 T49 E52 I75 N157 R159
BS02 FAD D N85 E86 N79 E80
BS03 DUR D E86 L87 S88 R90 E80 L81 S82 R84 MOAD: Kd=78uM
BS04 FAD D R78 H79 R80 I81 N169 L173 R174 H178 R72 H73 R74 I75 N163 L167 R168 H172
BS05 DUR D Q75 R78 R174 Q69 R72 R168 MOAD: Kd=78uM
Gene Ontology
Molecular Function
GO:0004799 thymidylate synthase activity
GO:0008168 methyltransferase activity
GO:0050660 flavin adenine dinucleotide binding
GO:0050797 thymidylate synthase (FAD) activity
GO:0070402 NADPH binding
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
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Biological Process
External links
PDB RCSB:5ioq, PDBe:5ioq, PDBj:5ioq
PDBsum5ioq
PubMed27214228
UniProtQ9WYT0|THYX_THEMA Flavin-dependent thymidylate synthase (Gene Name=thyX)

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