Structure of PDB 3o4v Chain B

Receptor sequence
>3o4vB (length=232) Species: 562 (Escherichia coli) [Search protein sequence]
MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGI
GKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDA
DVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDA
FINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVAD
QQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG
3D structure
PDB3o4v Crystal structure of E. coli MTA/SAH nucleosidase in complex with (4-Chlorophenyl)thio-DADMe-ImmA
ChainB
Resolution1.75 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 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 4CT B M9 I50 S76 A77 G78 F151 I152 E172 M173 E174 D197 F207 M9 I50 S76 A77 G78 F151 I152 E172 M173 E174 D197 F207 BindingDB: Kd=0.000047nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0008782 adenosylhomocysteine nucleosidase activity
GO:0008930 methylthioadenosine nucleosidase activity
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0009086 methionine biosynthetic process
GO:0009116 nucleoside metabolic process
GO:0009164 nucleoside catabolic process
GO:0019284 L-methionine salvage from S-adenosylmethionine
GO:0019509 L-methionine salvage from methylthioadenosine
GO:0046124 purine deoxyribonucleoside catabolic process
GO:0110052 toxic metabolite repair
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3o4v, PDBe:3o4v, PDBj:3o4v
PDBsum3o4v
PubMed
UniProtP0AF12|MTNN_ECOLI 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (Gene Name=mtnN)

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