Structure of PDB 1dyu Chain B Binding Site BS03

Receptor Information
>1dyu Chain B (length=720) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMVPMDKTLKEFGADVQWDDYAQLFTLIKDGAYVKVKPGAQTAIVNGQPL
ALQVPVVMKDNKAWVSDTFINDVFQSGLDQTFQVEKRPHPLNALTADEIK
QAVEIVKASADFKPNTRFTEISLLPPDKEAVWAFALENKPVDQPRKADVI
MLDGKHIIEAVVDLQNNKLLSWQPIKDAHGMVLLDDFASVQNIINNSEEF
AAAVKKRGITDAKKVITTPLTVGYFDGKDGLKQDARLLKVISYLDVGDGN
YWAHPIENLVAVVDLEQKKIVKIEEGPVVPVPMTARPFDGRDRVAPAVKP
MQIIEPEGKNYTITGDMIHWRNWDFHLSMNSRVGPMISTVTYNDNGTKRK
VMYEGSLGGMIVPYGDPDIGWYFKAYLDSGDYGMGTLTSPIARGKDAPSN
AVLLNETIADYTGVPMEIPRAIAVFERYAGPEYKHQEMGQPNVSTERREL
VVRWISTVGNYDYIFDWIFHENGTIGIDAGATGIEAVKGVKAKTMHDETA
KDDTRYGTLIDHNIVGTTHQHIYNFRLDLDVDGENNSLVAMDPVVKPNTA
GGPRTSTMQVNQYNIGNEQDAAQKFDPGTIRLLSNPNKENRMGNPVSYQI
IPYAGGTHPVAKGAQFAPDEWIYHRLSFMDKQLWVTRYHPGERFPEGKYP
NRSTHDTGLGQYSKDNESLDNTDAVVWMTTGTTHVARAEEWPIMPTEWVH
TLLKPWNFFDETPTLGALKK
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1dyu Chain B Residue 803 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1dyu The Active Site Base Controls Cofactor Reactivity in Escherichia Coli Amine Oxidase : X-Ray Crystallographicstudies with Mutational Variants
Resolution2.04 Å
Binding residue
(original residue number in PDB)		E573 H644 Y667 E672
Binding residue
(residue number reindexed from 1)		E568 H639 Y662 E667
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Y369 D383 Y466 H524 H526 H689
Catalytic site (residue number reindexed from 1) Y364 D378 Y461 H519 H521 H684
Enzyme Commision number 1.4.3.21: primary-amine oxidase.
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0005509 calcium 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:0006559 L-phenylalanine catabolic process
GO:0009308 amine metabolic process
GO:0019607 phenylethylamine catabolic process
Cellular Component
GO:0042597 periplasmic space

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1dyu, PDBe:1dyu, PDBj:1dyu
PDBsum1dyu
PubMed10387067
UniProtP46883|AMO_ECOLI Primary amine oxidase (Gene Name=tynA)

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