PPIRE04030

Target Protein Information
Protein_Name Macrophage metalloelastase
Protein_Sequence MSCTLLKGVCTMKFLMMIVFLQVSACGAAPMNDSEFAEWYLSRFYDYGKDRIPMTKTKTNRNFLKEKLQEMQQFFGLEATGQLDNSTLAIMHIPRCGVPDVQHLRAVPQRSRWMKRYLTYRIYNYTPDMKREDVDYIFQKAFQVWSDVTPLRFRKLHKDEADIMILFAFGAHGDFNYFDGKGGTLAHAFYPGPGIQGDAHFDEAETWTKSFQGTNLFLVAVHELGHSLGLQHSNNPKSIMYPTYRYLNPSTFRLSADDIRNIQSLYGAPVKPPSLTKPSSPPSTFCHQSLSFDAVTTVGEKIFFFKDWFFWWKLPGSPATNITSISSIWPSIPSGIQAAYEIESRNQLFLFKDEKYWLINNLVPEPHYPRSIYSLGFSASVKKVDAAVFDPLRQKVYFFVDKHYWRYDVRQELMDPAYPKLISTHFPGIKPKIDAVLYFKRHYYIFQGAYQLEYDPLFRRVTKTLKSTSWFGC
Organism_Source Mus musculus
Functional_Classification metalloproteases
Cellular_Localization Plasma membrane
Gene_Names Mmp12
UniProt_ID P34960
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name Thiorphan
Peptide_Sequence XG
Peptide_Length 2
Peptide_SMILES NCC(=O)NCC(=O)O
Chemical_Modification X1=3-mercapto-2-benzylpropanoyl
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification 3-Mercapto-2-Benzylpropanoyl
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 132.12
Aliphatic_Index 0.00000
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 -1.85410
Interaction Information
Affinity KD=4.7 nM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID None
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Rational design of enkephalinase inhibitors: substrate specificity of enkephalinase studied from inhibitory potency of various dipeptides.
Release_Year 1980
PMID 7004444
DOI 10.1016/0006-291x(80)91371-6