Structure of PDB 1ekm Chain B

Receptor sequence

>1ekmB (length=656)

APARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQ
WKEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPIL
TVEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGT
GKRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVS
KHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKF
HIGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRKH
ALDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCIH
EEDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQD
GAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRIDP
RIDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNYE
SATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPWA
SHSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILF
FHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTTS
EAKRAV

3D structure

• PDB: 1ekm Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli.
• Chain: B
• 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	ZN	B	Y405 H456 H458 H624	Y389 H440 H442 H608

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:1ekm, PDBe:1ekm, PDBj:1ekm
• PDBsum: 1ekm
• PubMed: 10933787
• UniProt: P12807|AMO_PICAN Peroxisomal primary amine oxidase (Gene Name=AMO)