Structure of PDB 1jys Chain A

Receptor sequence

>1jysA (length=226) Species: 562 (Escherichia coli)

MKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLKSGI
GKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARYHDA
DVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVSGDA
FINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISDVAD
QSFDEFLAVAAKQSSLMVESLVQKLA

3D structure

• PDB: 1jys Structure of E. coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase reveals similarity to the purine nucleoside phosphorylases.
• Chain: A
• Resolution: 1.9 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	ADE	A	F151 I152 E172 M173	F151 I152 E172 M173	MOAD: Ki=300uM PDBbind-CN: -logKd/Ki=3.52,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:1jys, PDBe:1jys, PDBj:1jys
• PDBsum: 1jys
• PubMed: 11591349
• UniProt: P0AF12|MTNN_ECOLI 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (Gene Name=mtnN)