Structure of PDB 6lug Chain B Binding Site BS01
Receptor Information
>6lug Chain B (length=273) Species:
1914
(Streptomyces lavendulae) [
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MIDLIVSQGRVADRAAWMIEGAARTARALEERYGLKGHYVGEPAPHADDD
WSVALPQARETLVAVREAATESIKGDNLTVLVNNTCSVSLATLPVVAREH
PDAVVLYIDGHGDFNTPETTDTGYLGGMVLSGACGLWDSGHGAGLRPEQA
VLVGSRDIDEGERELIRKAGVRVIPPGEATAQAVLDAVKDAPVWIHIDWD
VLEPGSIPADYTVPDGMLPAQIRAVFEAIPAERLIGVELAELNAPADSER
AEQAVAVILDMVAPAFDAAAARP
Ligand information
Ligand ID
MN
InChI
InChI=1S/Mn/q+2
InChIKey
WAEMQWOKJMHJLA-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mn+2]
CACTVS 3.341
[Mn++]
Formula
Mn
Name
MANGANESE (II) ION
ChEMBL
DrugBank
DB06757
ZINC
PDB chain
6lug Chain B Residue 401 [
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Receptor-Ligand Complex Structure
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PDB
6lug
Crystal structure of an Nomega-hydroxy-L-arginine hydrolase found in the D-cycloserine biosynthetic pathway.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
C86 D109 D113 D198
Binding residue
(residue number reindexed from 1)
C86 D109 D113 D198
Annotation score
1
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:6lug
,
PDBe:6lug
,
PDBj:6lug
PDBsum
6lug
PubMed
32496212
UniProt
D2Z025
|DCSB_STRLA N(omega)-hydroxy-L-arginine amidinohydrolase (Gene Name=dcsB)
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