Structure of PDB 1z5n Chain B

Receptor sequence

>1z5nB (length=232) Species: 562 (Escherichia coli)

MKIGIIGAMEEQVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGI
GKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDA
DVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDA
FINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVAD
QQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG

3D structure

• PDB: 1z5n Structural snapshots of MTA/AdoHcy nucleosidase along the reaction coordinate provide insights into enzyme and nucleoside flexibility during catalysis
• Chain: B
• Resolution: 2.1 Å

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	B	Q12 I50 S76 F151 M173 E174 R193 F207	Q12 I50 S76 F151 M173 E174 R193 F207
BS02	ADE	B	A77 G78 F151 I152 E172 M173 D197 A199	A77 G78 F151 I152 E172 M173 D197 A199	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

External links

• PDB: RCSB:1z5n, PDBe:1z5n, PDBj:1z5n
• PDBsum: 1z5n
• PubMed: 16109423
• UniProt: P0AF12|MTNN_ECOLI 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (Gene Name=mtnN)