Structure of PDB 2oqe Chain E

Receptor sequence
>2oqeE (length=657) [Search protein sequence]
AAPARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYI
QWKEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPI
LTVEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWG
TGKRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKV
SKHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFK
FHIGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRK
HALDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCI
HEEDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQ
DGAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRID
PRIDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNY
ESATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPW
ASHSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDIL
FFHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTT
SEAKRAV
3D structure
PDB2oqe Exploring molecular oxygen pathways in Hansenula polymorpha copper-containing amine oxidase
ChainE
Resolution1.6 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 H456 H458 H624 H441 H443 H609
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:2oqe, PDBe:2oqe, PDBj:2oqe
PDBsum2oqe
PubMed17409383
UniProtP12807|AMO_PICAN Peroxisomal primary amine oxidase (Gene Name=AMO)

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