Structure of PDB 1z5n Chain A

Receptor sequence
>1z5nA (length=234) Species: 562 (Escherichia coli) [Search protein sequence]
FSMKIGIIGAMEEQVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKS
GIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYH
DADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSG
DAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDV
ADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG
3D structure
PDB1z5n Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis
ChainA
Resolution2.1 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 SR1 A Q12 I50 F151 M173 E174 R193 F207 Q14 I52 F153 M175 E176 R195 F209
BS02 ADE A A77 G78 F151 I152 M173 D197 A79 G80 F153 I154 M175 D199 MOAD: Ki=300uM
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:1z5n, PDBe:1z5n, PDBj:1z5n
PDBsum1z5n
PubMed16109423
UniProtP0AF12|MTNN_ECOLI 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (Gene Name=mtnN)

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