Structure of PDB 5ioq Chain C

Receptor sequence
>5ioqC (length=218) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
HMKIDILDKGFVELVDVMGNDLSAVRAARVSFDLKDEERDRHLIEYLMKH
GHETPFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLSYEFYIP
SPERLEGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIVLP
LNLYTRFFWTVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCPWT
FEAFLKYAYKGDILKEVQ
3D structure
PDB5ioq Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase.
ChainC
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 C T55 E58 I81 N163 R165 T54 E57 I80 N162 R164
BS02 FAD C R78 H79 R80 I81 N169 L173 R174 H178 R77 H78 R79 I80 N168 L172 R173 H177
BS03 DUR C Q75 R78 R174 Q74 R77 R173 MOAD: Kd=78uM
BS04 FAD C N85 E86 N84 E85
BS05 DUR C E86 L87 S88 R90 E85 L86 S87 R89 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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