Structure of PDB 3n3y Chain D

Receptor sequence
>3n3yD (length=208) Species: 102617 (Helicobacter pylori SS1) [Search protein sequence]
MEVICKHYTPLDIASQAIRTCWQSFEYSDDGGCKDKELIHRVGNIFRHSS
TLEHLYYNFEIKGLSRGALQELSRHRIASLSVKSSRYTLRELKEVESFLP
LNETNLERAREFLVFVDNEKVNAMSVLALENLRVLLSEHNIKNDLAKYAM
PESYKTHLAYSINARSLQNLLTLRSSNKALKEMQDLAKALFDALPGEHQY
LFEDCLKH
3D structure
PDB3n3y Structure, Enzymatic Characterization and Inhibitor Discovery of Thymidylate Synthase X (ThyX) from Helicobacter pylori Strain SS1
ChainD
Resolution2.307 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 FAD D C21 R47 E53 I77 N163 R165 C21 R47 E53 I77 N163 R165
BS02 UMP D E71 R74 R174 E71 R74 R174
BS03 FAD D S81 V82 S81 V82
BS04 UMP D R66 S84 S85 R86 R66 S84 S85 R86
BS05 FAD D R74 H75 R76 I77 N169 R174 R74 H75 R76 I77 N169 R174
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:3n3y, PDBe:3n3y, PDBj:3n3y
PDBsum3n3y
PubMed
UniProtQ5UVJ4

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