Structure of PDB 1o2b Chain B

Receptor sequence
>1o2bB (length=215) Species: 2336 (Thermotoga maritima) [Search protein sequence]
MKIDILDKGFVELVDVMGNDLSAVRAARVSFDMERDRHLIEYLMKHGHET
PFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLSYEFYIPSPER
LEGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIVLPLNLY
TRFFWTVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCPWTFEAF
LKYAYKGDILKEVQV
3D structure
PDB1o2b Functional Analysis of Substrate and Cofactor Complex Structures of a Thymidylate Synthase-Complementing Protein
ChainB
Resolution2.45 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 B R78 H79 R80 I81 N169 L173 R174 H178 R73 H74 R75 I76 N164 L168 R169 H173
BS02 FAD B N85 E86 N80 E81
BS03 FAD B S30 E58 I81 N163 R165 S30 E53 I76 N158 R160
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:1o2b, PDBe:1o2b, PDBj:1o2b
PDBsum1o2b
PubMed12791256
UniProtQ9WYT0|THYX_THEMA Flavin-dependent thymidylate synthase (Gene Name=thyX)

[Back to BioLiP]