Structure of PDB 1nc3 Chain A

Receptor sequence

>1nc3A (length=235) Species: 562 (Escherichia coli)

EFSMKIGIIGAMEEEVTLLRDKIENRQTISLGGCEIYTGQLNGTEVALLK
SGIGKVAAALGATLLLEHCKPDVIINTGSAGGLAPTLKVGDIVVSDEARY
HDADVTAFGYEYGQLPGCPAGFKADDKLIAAAEACIAELNLNAVRGLIVS
GDAFINGSVGLAKIRHNFPQAIAVEMEATAIAHVCHNFNVPFVVVRAISD
VADQQSHLSFDEFLAVAAKQSSLMVESLVQKLAHG

3D structure

• PDB: 1nc3 Structure of Escherichia coli 5'-methylthioadenosine/ S-adenosylhomocysteine nucleosidase inhibitor complexes provide insight into the conformational changes required for substrate binding and catalysis.
• Chain: A
• Resolution: 2.2 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	FMC	A	S76 A77 G78 F151 I152 E172 M173 E174 D197 A199 F207	S79 A80 G81 F154 I155 E175 M176 E177 D200 A202 F210	MOAD: Ki=10uM PDBbind-CN: -logKd/Ki=5.00,Ki=10uM

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:1nc3, PDBe:1nc3, PDBj:1nc3
• PDBsum: 1nc3
• PubMed: 12496243
• UniProt: P0AF12|MTNN_ECOLI 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase (Gene Name=mtnN)