Structure of PDB 6nfp Chain B Binding Site BS02
Receptor Information
>6nfp Chain B (length=290) Species:
224308
(Bacillus subtilis subsp. subtilis str. 168) [
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NAMDKTISVIGMPMDLGQARRGVDMGPSAIRYAHLIERLSDMGYTVEDLG
DIPINELKNLNSVLAGNEKLAQKVNKVIEEKKFPLVLGGDHSIAIGTLAG
TAKHYDNLGVIWYDAHGDLNTLETSPSGNIHGMPLAVSLGIGHESLVNLE
GYAPKIKPENVVIIGARSLDEGERKYIKESGMKVYTMHEIDRLGMTKVIE
ETLDYLSACDGVHLSLDLDGLDPNDAPGVGTPVVGGISYRESHLAMEMLY
DAGIITSAEFVEVNPILDHKNKTGKTAVELVESLLGKKLL
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
6nfp Chain B Residue 304 [
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Receptor-Ligand Complex Structure
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PDB
6nfp
1.7 Angstrom Resolution Crystal Structure of Arginase from Bacillus subtilis subsp. subtilis str. 168
Resolution
1.7 Å
Binding residue
(original residue number in PDB)
H97 D120 D124 D223
Binding residue
(residue number reindexed from 1)
H91 D114 D118 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:6nfp
,
PDBe:6nfp
,
PDBj:6nfp
PDBsum
6nfp
PubMed
UniProt
P39138
|ARGI_BACSU Arginase (Gene Name=rocF)
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