Structure of PDB 1z5o Chain A

Receptor sequence
>1z5oA (length=235) Species: 562 (Escherichia coli) [Search protein sequence]
EFSMKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLK
SGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARY
HDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVS
GDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISN
VADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG
3D structure
PDB1z5o Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis
ChainA
Resolution2.0 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 MTA A S76 A77 F151 I152 E172 M173 E174 N197 F207 S79 A80 F154 I155 E175 M176 E177 N200 F210
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1z5o, PDBe:1z5o, PDBj:1z5o
PDBsum1z5o
PubMed16109423
UniProtP0AF12|MTNN_ECOLI 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (Gene Name=mtnN)

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