Structure of PDB 4bmz Chain B

Receptor sequence
>4bmzB (length=234) Species: 85962 (Helicobacter pylori 26695) [Search protein sequence]
GSHMVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVYHNKEII
VAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAGSLVKDLKINDLLVAIQ
LVQHDVDLSAFDHPLGFIPESAIFIETSESLNALAKEVANEQHIVLKEGV
IASGDQFVHSKERKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSI
SNNADEEANMSFDAFLEKSAQTSAKFLKSMVDEL
3D structure
PDB4bmz Structural Enzymology of Helicobacter Pylori Methylthioadenosine Nucleosidase in the Futalosine Pathway
ChainB
Resolution1.79 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.2.30: aminodeoxyfutalosine nucleosidase.
3.2.2.9: adenosylhomocysteine nucleosidase.
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 MTA B I53 V79 A80 G81 F154 V155 E174 M175 E176 R195 N199 F209 I56 V82 A83 G84 F157 V158 E177 M178 E179 R198 N202 F212
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008782 adenosylhomocysteine nucleosidase activity
GO:0008930 methylthioadenosine nucleosidase activity
GO:0016787 hydrolase activity
GO:0102246 6-amino-6-deoxyfutalosine hydrolase activity
Biological Process
GO:0009086 methionine biosynthetic process
GO:0009116 nucleoside metabolic process
GO:0009164 nucleoside catabolic process
GO:0009234 menaquinone biosynthetic process
GO:0019284 L-methionine salvage from S-adenosylmethionine
GO:0019509 L-methionine salvage from methylthioadenosine
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:4bmz, PDBe:4bmz, PDBj:4bmz
PDBsum4bmz
PubMed24419390
UniProtO24915|MQMTN_HELPY Aminodeoxyfutalosine nucleosidase (Gene Name=mtnN)

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