Structure of PDB 2oov Chain E

Receptor sequence
>2oovE (length=655) [Search protein sequence]
PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQW
KEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPILT
VEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGTG
KRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKFH
IGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRKHA
LDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCIHE
EDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRIDPR
IDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNYES
ATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPWAS
HSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTTSE
AKRAV
3D structure
PDB2oov Exploring molecular oxygen pathways in Hansenula polymorpha copper-containing amine oxidase
ChainE
Resolution1.7 Å
3D
structure
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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 E A405 H456 H458 H624 A388 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2oov, PDBe:2oov, PDBj:2oov
PDBsum2oov
PubMed17409383
UniProtP12807|AMO_PICAN Peroxisomal primary amine oxidase (Gene Name=AMO)

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