Structure of PDB 1a2v Chain E Binding Site BS01

Receptor Information
>1a2v Chain E (length=655) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
PARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQW
KEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPILT
VEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGTG
KRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVSK
HKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKFH
IGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRKHA
LDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCIHE
EDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQDG
AIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRIDPR
IDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNYES
ATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPWAS
HSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILFF
HTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTTSE
AKRAV
Ligand information
Ligand IDCU
InChIInChI=1S/Cu/q+2
InChIKeyJPVYNHNXODAKFH-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Cu+2]
CACTVS 3.341[Cu++]
FormulaCu
NameCOPPER (II) ION
ChEMBL
DrugBankDB14552
ZINC
PDB chain1a2v Chain E Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1a2v Crystallographic study of yeast copper amine oxidase.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		H456 H458 H624
Binding residue
(residue number reindexed from 1)		H439 H441 H607
Annotation score1
Enzymatic activity
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1a2v, PDBe:1a2v, PDBj:1a2v
PDBsum1a2v
PubMed15299901
UniProtP12807|AMO_PICAN Peroxisomal primary amine oxidase (Gene Name=AMO)

[Back to BioLiP]