PPIRE05026

Target Protein Information
Protein_Name Stromelysin-1
Protein_Sequence MKSLPILLLLCVAVCSAYPLDGAARGEDTSMNLVQKYLENYYDLKKDVKQFVRRKDSGPVVKKIREMQKFLGLEVTGKLDSDTLEVMRKPRCGVPDVGHFRTFPGIPKWRKTHLTYRIVNYTPDLPKDAVDSAVEKALKVWEEVTPLTFSRLYEGEADIMISFAVREHGDFYPFDGPGNVLAHAYAPGPGINGDAHFDDDEQWTKDTTGTNLFLVAAHEIGHSLGLFHSANTEALMYPLYHSLTDLTRFRLSQDDINGIQSLYGPPPDSPETPLVPTEPVPPEPGTPANCDPALSFDAVSTLRGEILIFKDRHFWRKSLRKLEPELHLISSFWPSLPSGVDAAYEVTSKDLVFIFKGNQFWAIRGNEVRAGYPRGIHTLGFPPTVRKIDAAISDKEKNKTYFFVEDKYWRFDEKRNSMEPGFPKQIAEDFPGIDSKIDAVFEEFGFFYFFTGSSQLEFDPNAKKVTHTLKSNSWLNC
Organism_Source Homo sapiens
Functional_Classification matrix metalloproteinases
Cellular_Localization Extracellular
Gene_Names MMP3
UniProt_ID P08254
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name Ac-PRCG-NH2
Peptide_Sequence PRCG
Peptide_Length 4
Peptide_SMILES N=C(N)NCCC[C@H](NC(=O)[C@@H]1CCCN1)C(=O)N[C@@H](CS)C(=O)NCC(=O)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Acetyl
C-terminal_Modification amide
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 431.51
Aliphatic_Index 0.00000
Aromaticity 0.00000
Average_Rotatable_Bonds 3.00000
Charge_at_pH_7 0.93601
Isoelectric_Point 8.54991
Number_of_Hydrogen_Bond_Acceptors 7
Number_of_Hydrogen_Bond_Donors 9
Topological_Polar_Surface_Area 198.53000
X_logP_energy -2.89813
Interaction Information
Affinity IC50=500 uM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID None
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Peptides based on the conserved predomain sequence of matrix metalloproteinases inhibit human stromelysin and collagenase.
Release_Year 1993
PMID 8273554
DOI 10.1007/bf01972749