Structure of PDB 1cev Chain C Binding Site BS02
Receptor Information
>1cev Chain C (length=299) Species:
33931
([Bacillus] caldovelox) [
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MKPISIIGVPMDLGQTRRGVDMGPSAMRYAGVIERLERLHYDIEDLGDIP
IGKAERLHEQGDSRLRNLKAVAEANEKLAAAVDQVVQRGRFPLVLGGDHS
IAIGTLAGVAKHYERLGVIWYDAHGDVNTAETSPSGNIHGMPLAASLGFG
HPALTQIGGYSPKIKPEHVVLIGVRSLDEGEKKFIREKGIKIYTMHEVDR
LGMTRVMEETIAYLKERTDGVHLSLDLDGLDPSDAPGVGTPVIGGLTYRE
SHLAMEMLAEAQIITSAEFVEVNPILDERNKTASVAVALMGSLFGEKLM
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
1cev Chain C Residue 301 [
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Receptor-Ligand Complex Structure
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PDB
1cev
Crystal structures of Bacillus caldovelox arginase in complex with substrate and inhibitors reveal new insights into activation, inhibition and catalysis in the arginase superfamily.
Resolution
2.4 Å
Binding residue
(original residue number in PDB)
D122 H124 D226 D228
Binding residue
(residue number reindexed from 1)
D122 H124 D226 D228
Annotation score
1
Enzymatic activity
Catalytic site (original residue number in PDB)
H99 D122 H124 D126 H139 D226 D228 E271
Catalytic site (residue number reindexed from 1)
H99 D122 H124 D126 H139 D226 D228 E271
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:1cev
,
PDBe:1cev
,
PDBj:1cev
PDBsum
1cev
PubMed
10196128
UniProt
P53608
|ARGI_BACCD Arginase (Gene Name=rocF)
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