Structure of PDB 1o27 Chain C

Receptor sequence
>1o27C (length=216) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKIDILDKGFVELVDVMGNDLSAVRAARVSFKDEERDRHLIEYLMKHGHE
TPFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLSYEFYIPSPE
RLEGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIVLPLNL
YTRFFWTVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCPWTFEA
FLKYAYKGDILKEVQV
3D structure
PDB1o27 Functional Analysis of Substrate and Cofactor Complex Structures of a Thymidylate Synthase-Complementing Protein
ChainC
Resolution2.3 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 T51 E54 I77 N159 R161
BS02 BRU C Q75 R78 R174 Q71 R74 R170
BS03 FAD C N85 E86 N81 E82
BS04 FAD C R78 H79 R80 I81 N169 L173 H178 R74 H75 R76 I77 N165 L169 H174
BS05 BRU C E86 S88 G89 R90 Y91 R147 E82 S84 G85 R86 Y87 R143
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1o27, PDBe:1o27, PDBj:1o27
PDBsum1o27
PubMed12791256
UniProtQ9WYT0|THYX_THEMA Flavin-dependent thymidylate synthase (Gene Name=thyX)

[Back to BioLiP]