Structure of PDB 3t0u Chain C Binding Site BS01

Receptor Information
>3t0u Chain C (length=665) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AAPARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYI
QWKEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPI
LTVEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWG
TGKRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKV
SKHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFK
FHIGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRK
HALDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCI
HEEDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQ
DGAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRID
PRIDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNY
ESATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPW
ASHSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDIL
FFHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTT
SEAKRAVAFEGSCCG
Ligand information
Ligand IDCU1
InChIInChI=1S/Cu/q+1
InChIKeyVMQMZMRVKUZKQL-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
CACTVS 3.341
OpenEye OEToolkits 1.5.0		[Cu+]
FormulaCu
NameCOPPER (I) ION
ChEMBL
DrugBank
ZINC
PDB chain3t0u Chain C Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3t0u The precursor form of Hansenula polymorpha copper amine oxidase 1 in complex with CuI and CoII.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		Y405 H456 H458 H624
Binding residue
(residue number reindexed from 1)		Y390 H441 H443 H609
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y305 D319 Y405 H456 H458 H624
Catalytic site (residue number reindexed from 1) Y290 D304 Y390 H441 H443 H609
Enzyme Commision number 1.4.3.21: primary-amine oxidase.
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:3t0u, PDBe:3t0u, PDBj:3t0u
PDBsum3t0u
PubMed22691777
UniProtP12807|AMO_PICAN Peroxisomal primary amine oxidase (Gene Name=AMO)

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