Structure of PDB 1o25 Chain C

Receptor sequence
>1o25C (length=217) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKIDILDKGFVELVDVMGNDLSAVRAARVSFDKDEERDRHLIEYLMKHGH
ETPFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLSYEFYIPSP
ERLEGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIVLPLN
LYTRFFWTVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCPWTFE
AFLKYAYKGDILKEVQV
3D structure
PDB1o25 Functional Analysis of Substrate and Cofactor Complex Structures of a Thymidylate Synthase-Complementing Protein
ChainC
Resolution2.4 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 UMP C Q75 R78 R174 Q72 R75 R171
BS02 UMP C E86 S88 G89 R90 R147 E83 S85 G86 R87 R144
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:1o25, PDBe:1o25, PDBj:1o25
PDBsum1o25
PubMed12791256
UniProtQ9WYT0|THYX_THEMA Flavin-dependent thymidylate synthase (Gene Name=thyX)

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