Structure of PDB 3ah5 Chain A

Receptor sequence
>3ah5A (length=215) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
MEVICKHYTPLDIASQAIRTCWQSFEYSDDGGCKDKELIHRVGNIFRHSS
TLEHLYYNFEIKGLSRGALQELSRHRIASLSVKSSRYTLRELKEVESFLP
LNETNLERAKEFLVFVDNEKVNAMSVLALENLRILLSEHNIKNDLAKYAM
PESYKTHLAYSINARSLQNFLTLRSSNKALKEMQDLAKALFDALPGEHQY
LFEDCLKHLEHHHHH
3D structure
PDB3ah5 Crystal structure and functional analysis of a flavin dependent thymidylate synthase from helicobacter pylori
ChainA
Resolution2.5 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 UMP A R89 S107 S108 R109 R66 S84 S85 R86
BS02 FAD A R97 H98 R99 I100 N192 L196 R197 K201 R74 H75 R76 I77 N169 L173 R174 K178
BS03 FAD A C44 R70 H71 S73 E76 I100 N186 R188 C21 R47 H48 S50 E53 I77 N163 R165
BS04 FAD A S104 V105 Y110 S81 V82 Y87
BS05 UMP A E94 R97 R197 E71 R74 R174
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:3ah5, PDBe:3ah5, PDBj:3ah5
PDBsum3ah5
PubMed
UniProtO26061|THYX_HELPY Flavin-dependent thymidylate synthase (Gene Name=thyX)

[Back to BioLiP]