Structure of PDB 6nbk Chain D Binding Site BS02
Receptor Information
>6nbk Chain D (length=287) Species:
1431339
(Bacillus thuringiensis DB27) [
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KEISVIGVPMDLGQMRRGVDMGPSAIRYAGVIERIEEIGYDVKDMGDICI
ENTKLRNLTQVATVCNELASKVDHIIEEGRFPLVLGGDHSIAIGTLAGVA
KHYKNLGVIWYDAHGDLNTEETSPSGNIHGMSLAASLGYGHSSLVDLYGA
YPKVKKENVVIIGARALDEGEKDFIRNEGIKVFSMHEIDRMGMTAVMEET
IAYLSHTDGVHLSLDLDGLDPHDAPGVGTPVIGGLSYRESHLAMEMLAEA
DIITSAEFVEVNTILDERNRTATTAVALMGSLFGEKL
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
6nbk Chain D Residue 302 [
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Receptor-Ligand Complex Structure
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PDB
6nbk
Crystal structure of Arginase from Bacillus cereus
Resolution
1.91 Å
Binding residue
(original residue number in PDB)
D121 H123 D224 D226
Binding residue
(residue number reindexed from 1)
D112 H114 D215 D217
Annotation score
1
Enzymatic activity
Enzyme Commision number
3.5.3.1
: arginase.
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:0000050
urea cycle
GO:0006525
arginine metabolic process
GO:0019547
arginine catabolic process to ornithine
Cellular Component
GO:0005737
cytoplasm
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:6nbk
,
PDBe:6nbk
,
PDBj:6nbk
PDBsum
6nbk
PubMed
UniProt
W8YSI5
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