Structure of PDB 8ius Chain A Binding Site BS02

Receptor Information
>8ius Chain A (length=272) 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
AEQAVAVILDMVAPAFDAAAAR
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain8ius Chain A Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB8ius Copper inactivates DcsB by oxidation of the Cys86 to cysteine sulfinic aicd
Resolution2.14 Å
Binding residue
(original residue number in PDB)
D109 H111 D198 D200
Binding residue
(residue number reindexed from 1)
D109 H111 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:8ius, PDBe:8ius, PDBj:8ius
PDBsum8ius
PubMed
UniProtD2Z025|DCSB_STRLA N(omega)-hydroxy-L-arginine amidinohydrolase (Gene Name=dcsB)

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