Structure of PDB 1o26 Chain B

Receptor sequence
>1o26B (length=221) Species: 2336 (Thermotoga maritima) [Search protein sequence]
HMKIDILDKGFVELVDVMGNDLSAVRAARVSFDMGLKDEERDRHLIEYLM
KHGHETPFEHIVFTFHVKAPIFVARQWFRHRIASYNELSGRYSKLSYEFY
IPSPERLEGYKTTIPPERVTEKISEIVDKAYRTYLELIESGVPREVARIV
LPLNLYTRFFWTVNARSLMNFLNLRADSHAQWEIQQYALAIARIFKEKCP
WTFEAFLKYAYKGDILKEVQV
3D structure
PDB1o26 Functional Analysis of Substrate and Cofactor Complex Structures of a Thymidylate Synthase-Complementing Protein
ChainB
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 UMP B E86 S88 G89 R90 R147 E87 S89 G90 R91 R148
BS02 FAD B R78 H79 R80 I81 N169 L173 R174 H178 R79 H80 R81 I82 N170 L174 R175 H179
BS03 FAD B N85 E86 N86 E87
BS04 UMP B Q75 R78 R174 Q76 R79 R175
BS05 FAD B S30 T55 E58 I81 N163 R165 S31 T56 E59 I82 N164 R166
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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