Structure of PDB 4n09 Chain A

Receptor sequence

>4n09A (length=345)

MSSAPLRVYVQCNPLLDVSAHVSDEFLVKYGLERGTAILLSERQKGIFDD
IEKMPNVRYVPGGSGLNVARVAQWMQQAYKGKFVTYVGCIADDRYGKVLK
EAAEHEGIVMAVEHTTKAGSGACAVCITGKERTLVADLGAANHLSSEHMR
SPAVVRAMDESRIFYFSGFTLTVDVNHVLQACRKAREVDGLFMINLSAPF
IMQFFSAQLGEVLPYTDIIVANRHEAKEFANMMKWDTDCVEEIARRAVSE
VPYTGTKGRVVVFTRDIESTVLATKDGVETVPVPQLDQDKVIDMNGAGDA
FMGGFLSAYAVGKDLRRCCETGHYTAQEVIQRDGCSFPEKPSFSP

3D structure

• PDB: 4n09 Structures of adenosine kinase from Trypanosoma brucei brucei.
• Chain: A
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R132 D299
• Catalytic site (residue number reindexed from 1): R132 D299
• Enzyme Commision number: 2.7.1.20: adenosine kinase.

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	ADN	A	N13 L15 D17 G63 S64 C123 A136 F169 D299	N13 L15 D17 G63 S64 C123 A136 F169 D299
BS02	ADP	A	N222 T264 D266 Q288 A297 G298 A326 Q327 I330	N222 T264 D266 Q288 A297 G298 A326 Q327 I330

Gene Ontology

Molecular Function

• GO:0004001 adenosine kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity

Biological Process

• GO:0006144 purine nucleobase metabolic process
• GO:0006166 purine ribonucleoside salvage
• GO:0009152 purine ribonucleotide biosynthetic process
• GO:0016310 phosphorylation
• GO:0044209 AMP salvage

Cellular Component

• GO:0005634 nucleus
• GO:0005654 nucleoplasm
• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0020015 glycosome
• GO:0097014 ciliary plasm

External links

• PDB: RCSB:4n09, PDBe:4n09, PDBj:4n09
• PDBsum: 4n09
• PubMed: 24419613
• UniProt: Q584S0