Structure of PDB 1o26 Chain C

Receptor sequence
>1o26C (length=218) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKIDILDKGFVELVDVMGNDLSAVRAARVSFDMGLKDEERDRHLIEYLMK
HGHETPFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLSYEFYI
PSPERLEGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIVL
PLNLYTRFFWTVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCPW
TFEAFLKYAYKGDILKEV
3D structure
PDB1o26 Functional Analysis of Substrate and Cofactor Complex Structures of a Thymidylate Synthase-Complementing Protein
ChainC
Resolution1.6 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 S30 T55 E58 I81 N163 R165 S30 T55 E58 I81 N163 R165
BS02 UMP C R74 Q75 R78 R174 R74 Q75 R78 R174
BS03 FAD C N85 E86 N85 E86
BS04 FAD C R78 H79 R80 I81 N169 L173 R174 H178 R78 H79 R80 I81 N169 L173 R174 H178
BS05 UMP C E86 S88 G89 R90 R147 E86 S88 G89 R90 R147
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:1o26, PDBe:1o26, PDBj:1o26
PDBsum1o26
PubMed12791256
UniProtQ9WYT0|THYX_THEMA Flavin-dependent thymidylate synthase (Gene Name=thyX)

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