Structure of PDB 6nfp Chain B Binding Site BS02

Receptor Information
>6nfp Chain B (length=290) Species: 224308 (Bacillus subtilis subsp. subtilis str. 168) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NAMDKTISVIGMPMDLGQARRGVDMGPSAIRYAHLIERLSDMGYTVEDLG
DIPINELKNLNSVLAGNEKLAQKVNKVIEEKKFPLVLGGDHSIAIGTLAG
TAKHYDNLGVIWYDAHGDLNTLETSPSGNIHGMPLAVSLGIGHESLVNLE
GYAPKIKPENVVIIGARSLDEGERKYIKESGMKVYTMHEIDRLGMTKVIE
ETLDYLSACDGVHLSLDLDGLDPNDAPGVGTPVVGGISYRESHLAMEMLY
DAGIITSAEFVEVNPILDHKNKTGKTAVELVESLLGKKLL
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 chain6nfp Chain B Residue 304 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6nfp 1.7 Angstrom Resolution Crystal Structure of Arginase from Bacillus subtilis subsp. subtilis str. 168
Resolution1.7 Å
Binding residue
(original residue number in PDB)
H97 D120 D124 D223
Binding residue
(residue number reindexed from 1)
H91 D114 D118 D217
Annotation score1
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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Cellular Component
External links
PDB RCSB:6nfp, PDBe:6nfp, PDBj:6nfp
PDBsum6nfp
PubMed
UniProtP39138|ARGI_BACSU Arginase (Gene Name=rocF)

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