Structure of PDB 3n9h Chain A

Receptor sequence

>3n9hA (length=655)

PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQW
KEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPILT
VEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGTG
KRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKFH
IGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPAGSPEFPHQRKHA
LDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCIHE
EDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRIDPR
IDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNYES
ATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPWAS
HSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTTSE
AKRAV

3D structure

• PDB: 3n9h Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.
• Chain: A
• Resolution: 2.5 Å

Enzymatic activity

• Enzyme Commision number: 1.4.3.21: primary-amine oxidase.

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	CU	A	H456 H458 H624	H439 H441 H607

Gene Ontology

Molecular Function

• GO:0005507 copper ion binding
• GO:0008131 primary methylamine oxidase activity
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding
• GO:0048038 quinone binding
• GO:0052595 aliphatic amine oxidase activity

Biological Process

• GO:0009308 amine metabolic process

Cellular Component

• GO:0005777 peroxisome

External links

• PDB: RCSB:3n9h, PDBe:3n9h, PDBj:3n9h
• PDBsum: 3n9h
• PubMed: 20684524
• UniProt: P12807|AMO_PICAN Peroxisomal primary amine oxidase (Gene Name=AMO)