Structure of PDB 3n3y Chain A

Receptor sequence
>3n3yA (length=209) Species: 102617 (Helicobacter pylori SS1) [Search protein sequence]
FMEVICKHYTPLDIASQAIRTCWQSFEYSDDGGCKDKELIHRVGNIFRHS
STLEHLYYNFEIKGLSRGALQELSRHRIASLSVKSSRYTLRELKEVESFL
PLNETNLERAREFLVFVDNEKVNAMSVLALENLRVLLSEHNIKNDLAKYA
MPESYKTHLAYSINARSLQNLLTLRSSNKALKEMQDLAKALFDALPGEHQ
YLFEDCLKH
3D structure
PDB3n3y Structure, Enzymatic Characterization and Inhibitor Discovery of Thymidylate Synthase X (ThyX) from Helicobacter pylori Strain SS1
ChainA
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 UMP A H7 Y8 P10 H8 Y9 P11
BS02 FAD A R74 H75 R76 I77 N169 R174 R75 H76 R77 I78 N170 R175
BS03 UMP A R66 V82 S84 S85 R86 K147 R67 V83 S85 S86 R87 K148
BS04 UMP A E71 R74 R174 E72 R75 R175
BS05 FAD A S81 V82 S82 V83
BS06 FAD A R47 E53 I77 N163 R165 R48 E54 I78 N164 R166
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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