Structure of PDB 8iuw Chain B Binding Site BS02

Receptor Information
>8iuw Chain B (length=274) Species: 1914 (Streptomyces lavendulae) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MIDLIVSQGRVADRAAWMIEGAARTARALEERYGLKGHYVGEPAPHADDD
WSVALPQARETLVAVREAATESIKGDNLTVLVNNTCSVSLATLPVVAREH
PDAVVLYIDGHGDFNTPETTDTGYLGGMVLSGACGLWDSGHGAGLRPEQA
VLVGSRDIDEGERELIRKAGVRVIPPGEATAQAVLDAVKDAPVWIHIDWD
VLEPGSIPADYTVPDGMLPAQIRAVFEAIPAERLIGVELAELNAPADSER
AEQAVAVILDMVAPAFDAAAARPL
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 chain8iuw Chain B Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8iuw Copper inactivates DcsB by oxidation of the Cys86 to cysteine sulfinic aicd
Resolution1.5 Å
Binding residue
(original residue number in PDB)		D109 D198 D200
Binding residue
(residue number reindexed from 1)		D109 D198 D200
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.3.25: N(omega)-hydroxy-L-arginine amidinohydrolase.
Gene Ontology
Molecular Function
GO:0004053 arginase activity
GO:0016787 hydrolase activity
GO:0016813 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
GO:0030145 manganese ion binding
GO:0046872 metal ion binding
Biological Process
GO:0017000 antibiotic biosynthetic process
GO:0019547 arginine catabolic process to ornithine
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8iuw, PDBe:8iuw, PDBj:8iuw
PDBsum8iuw
PubMed
UniProtD2Z025|DCSB_STRLA N(omega)-hydroxy-L-arginine amidinohydrolase (Gene Name=dcsB)

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