Structure of PDB 1ekm Chain B Binding Site BS01

Receptor Information
>1ekm Chain B (length=656) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
APARPAHPLDPLSTAEIKAATNTVKSYFAGKKISFNTVTLREPARKAYIQ
WKEQGGPLPPRLAYYVILEAGKPGVKEGLVDLASLSVIETRALETVQPIL
TVEDLCSTEEVIRNDPAVIEQCVLSGIPANEMHKVYCDPWTIGYDERWGT
GKRLQQALVYYRSDEDDSQYSHPLDFCPIVDTEEKKVIFIDIPNRRRKVS
KHKHANFYPKHMIEKVGAMRPEAPPINVTQPEGVSFKMTGNVMEWSNFKF
HIGFNYREGIVLSDVSYNDHGNVRPIFHRISLSEMIVPYGSPEFPHQRKH
ALDIGEYGAGYMTNPLSLGCDCKGVIHYLDAHFSDRAGDPITVKNAVCIH
EEDDGLLFKHSDFRDNFATSLVTRATKLVVSQIFTAANYEYCLYWVFMQD
GAIRLDIRLTGILNTYILGDDEEAGPWGTRVYPNVNAHNHQHLFSLRIDP
RIDGDGNSAAACDAKSSPYPLGSPENMYGNAFYSEKTTFKTVKDSLTNYE
SATGRSWDIFNPNKVNPYSGKPPSYKLVSTQCPPLLAKEGSLVAKRAPWA
SHSVNVVPYKDNRLYPSGDHVPQWSGDGVRGMREWIGDGSENIDNTDILF
FHTFGITHFPAPEDFPLMPAEPITLMLRPRHFFTENPGLDIQPSYAMTTS
EAKRAV
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain1ekm Chain B Residue 701 [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]
PDB1ekm Crystal structure at 2.5 A resolution of zinc-substituted copper amine oxidase of Hansenula polymorpha expressed in Escherichia coli.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		Y405 H456 H458 H624
Binding residue
(residue number reindexed from 1)		Y389 H440 H442 H608
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:1ekm, PDBe:1ekm, PDBj:1ekm
PDBsum1ekm
PubMed10933787
UniProtP12807|AMO_PICAN Peroxisomal primary amine oxidase (Gene Name=AMO)

[Back to BioLiP]