PPIRE03804

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 Phe-Met
Peptide_Sequence FM
Peptide_Length 2
Peptide_SMILES CSCC[C@H](NC(=O)[C@@H](N)Cc1ccccc1)C(=O)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 296.38
Aliphatic_Index 0.00000
Aromaticity 0.50000
Average_Rotatable_Bonds 4.00000
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 4
Number_of_Hydrogen_Bond_Donors 3
Topological_Polar_Surface_Area 92.42000
X_logP_energy 0.87890
Interaction Information
Affinity IC50=8.6 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