PPIRE03756

Target Protein Information
Protein_Name Macrophage metalloelastase
Protein_Sequence MSCTLLKGVCTMKFLMMIVFLQVSACGAAPMNDSEFAEWYLSRFYDYGKDRIPMTKTKTNRNFLKEKLQEMQQFFGLEATGQLDNSTLAIMHIPRCGVPDVQHLRAVPQRSRWMKRYLTYRIYNYTPDMKREDVDYIFQKAFQVWSDVTPLRFRKLHKDEADIMILFAFGAHGDFNYFDGKGGTLAHAFYPGPGIQGDAHFDEAETWTKSFQGTNLFLVAVHELGHSLGLQHSNNPKSIMYPTYRYLNPSTFRLSADDIRNIQSLYGAPVKPPSLTKPSSPPSTFCHQSLSFDAVTTVGEKIFFFKDWFFWWKLPGSPATNITSISSIWPSIPSGIQAAYEIESRNQLFLFKDEKYWLINNLVPEPHYPRSIYSLGFSASVKKVDAAVFDPLRQKVYFFVDKHYWRYDVRQELMDPAYPKLISTHFPGIKPKIDAVLYFKRHYYIFQGAYQLEYDPLFRRVTKTLKSTSWFGC
Organism_Source Mus musculus
Functional_Classification metalloendopeptidases
Cellular_Localization Plasma membrane
Gene_Names Mmp12
UniProt_ID P34960
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name HO-NHCOCH2-CO-Ala-Gly-NH2
Peptide_Sequence AG
Peptide_Length 2
Peptide_SMILES C[C@H](N)C(=O)NCC(=O)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Ho-Nhcoch2-Co
C-terminal_Modification amide
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 146.15
Aliphatic_Index 50.00000
Aromaticity 0.00000
Average_Rotatable_Bonds 1.50000
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 3
Number_of_Hydrogen_Bond_Donors 3
Topological_Polar_Surface_Area 92.42000
X_logP_energy -1.46560
Interaction Information
Affinity IC50=41 uM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID None
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Enkephalinase: selective peptide inhibitors.
Release_Year 1981
PMID 7033704
DOI 10.1016/0024-3205(81)90632-9