Structure of PDB 3nbb Chain D

Receptor sequence

>3nbbD (length=661)

SAAPARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAY
IQWKEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQP
ILTVEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERW
GTGKRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRK
VSKHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNF
KFHIGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPFGSPEFPHQR
KHALDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVC
IHEEDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFM
QDGAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRI
DPRIDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTN
YESATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAP
WASHSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDI
LFFHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMT
TSEAKRAVHKE

3D structure

• PDB: 3nbb Mutation at a strictly conserved, active site tyrosine in the copper amine oxidase leads to uncontrolled oxygenase activity.
• Chain: D
• Resolution: 2.05 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	D	H456 H458 H624	H442 H444 H610

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