Structure of PDB 7euk Chain A Binding Site BS01

Receptor Information
>7euk Chain A (length=271) 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
AEQAVAVILDMVAPAFDAAAA
Ligand information
Ligand IDMN
InChIInChI=1S/Mn/q+2
InChIKeyWAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341[Mn++]
FormulaMn
NameMANGANESE (II) ION
ChEMBL
DrugBankDB06757
ZINC
PDB chain7euk Chain A Residue 401 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7euk Catalytic mechanism of DcsB: Arginase framework used for hydrolyzing its inhibitor.
Resolution1.4 Å
Binding residue
(original residue number in PDB)
C86 D109 D113 D198
Binding residue
(residue number reindexed from 1)
C86 D109 D113 D198
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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Biological Process

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Cellular Component
External links
PDB RCSB:7euk, PDBe:7euk, PDBj:7euk
PDBsum7euk
PubMed35634777
UniProtD2Z025|DCSB_STRLA N(omega)-hydroxy-L-arginine amidinohydrolase (Gene Name=dcsB)

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