Structure of PDB 4ev5 Chain E

Receptor sequence
>4ev5E (length=654) Species: 870730 (Ogataea angusta) [Search protein sequence]
ARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQWK
EQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPILTV
EDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGTGK
RLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSKH
KHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKFHI
GFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRKHAL
DIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCIHEE
DDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQDGA
IRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRIDPRI
DGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNYESA
TGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPWASH
SVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFFH
TFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTTSEA
KRAV
3D structure
PDB4ev5 Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with benzylamine
ChainE
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Y305 D319 Y405 H456 H458 H624
Catalytic site (residue number reindexed from 1) Y287 D301 Y387 H438 H440 H606
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 H438 H440 H606
BS02 ABN E W156 A317 D319 Y323 A402 A403 Y405 W138 A299 D301 Y305 A384 A385 Y387
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4ev5, PDBe:4ev5, PDBj:4ev5
PDBsum4ev5
PubMed
UniProtP12807|AMO_PICAN Peroxisomal primary amine oxidase (Gene Name=AMO)

[Back to BioLiP]