Structure of PDB 5ios Chain D

Receptor sequence
>5iosD (length=217) Species: 243274 (Thermotoga maritima MSB8) [Search protein sequence]
MKIDILDKGFVELVDVMGNDLSAVRAARVSFDMLKDEERDRHLIEYLMKH
GHETPFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGAYSKLSYEFYIP
SPERLEGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIVLP
LNLYTRFFWTVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCPWT
FEAFLKYAYKGDILKEV
3D structure
PDB5ios Deprotonations in the Reaction of Flavin-Dependent Thymidylate Synthase.
ChainD
Resolution1.9 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 S30 T55 E58 I81 N163 R165 S30 T54 E57 I80 N162 R164
BS02 FAD D N85 E86 N84 E85
BS03 UMP D R74 Q75 R78 R174 R73 Q74 R77 R173 MOAD: Kd=14uM
BS04 FAD D R78 H79 R80 I81 N169 L173 R174 H178 R77 H78 R79 I80 N168 L172 R173 H177
BS05 UMP D E86 S88 G89 A90 R147 E85 S87 G88 A89 R146 MOAD: Kd=14uM
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:5ios, PDBe:5ios, PDBj:5ios
PDBsum5ios
PubMed27214228
UniProtQ9WYT0|THYX_THEMA Flavin-dependent thymidylate synthase (Gene Name=thyX)

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