Structure of PDB 1o29 Chain D

Receptor sequence
>1o29D (length=215) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKIDILDKGFVELVDVMGNDLSAVRAARVSFDMDEERDRHLIEYLMKHGH
ETPFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLSYEFYIPSP
ERLEGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIVLPLN
LYTRFFWTVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCPWTFE
AFLKYAYKGDILKEV
3D structure
PDB1o29 Functional Analysis of Substrate and Cofactor Complex Structures of a Thymidylate Synthase-Complementing Protein
ChainD
Resolution2.0 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 UFP D Q75 R78 R174 Q72 R75 R171
BS02 FAD D N85 E86 Y91 N82 E83 Y88
BS03 FAD D S30 H53 T55 E58 I81 N163 R165 S30 H50 T52 E55 I78 N160 R162
BS04 FAD D R78 H79 R80 I81 N169 L173 H178 R75 H76 R77 I78 N166 L170 H175
BS05 UFP D 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:1o29, PDBe:1o29, PDBj:1o29
PDBsum1o29
PubMed12791256
UniProtQ9WYT0|THYX_THEMA Flavin-dependent thymidylate synthase (Gene Name=thyX)

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