Structure of PDB 6nbk Chain B Binding Site BS02

Receptor Information
>6nbk Chain B (length=287) Species: 1431339 (Bacillus thuringiensis DB27) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KEISVIGVPMDLGQMRRGVDMGPSAIRYAGVIERIEEIGYDVKDMGDICI
NTKLRNLTQVATVCNELASKVDHIIEEGRFPLVLGGDHSIAIGTLAGVAK
HYKNLGVIWYDAHGDLNTEETSPSGNIHGMSLAASLGYGHSSLVDLYGAY
PKVKKENVVIIGARALDEGEKDFIRNEGIKVFSMHEIDRMGMTAVMEETI
AYLSHTDGVHLSLDLDGLDPHDAPGVGTPVIGGLSYRESHLAMEMLAEAD
IITSAEFVEVNTILDERNRTATTAVALMGSLFGEKLK
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 chain6nbk Chain B Residue 302 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB6nbk Crystal structure of Arginase from Bacillus cereus
Resolution1.91 Å
Binding residue
(original residue number in PDB)
D121 H123 D224 D226
Binding residue
(residue number reindexed from 1)
D111 H113 D214 D216
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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6nbk, PDBe:6nbk, PDBj:6nbk
PDBsum6nbk
PubMed
UniProtW8YSI5

[Back to BioLiP]