PPIRE11583

Target Protein Information
Protein_Name Cerebral cavernous malformations 2 protein
Protein_Sequence MEEEGKKGKKPGIVSPFKRVFLKGEKSRDKKAHEKVTERRPLHTVVLSLPERVEPDRLLSDYIEKEVKYLGQLTSIPGYLNPSSRTEILHFIDNAKRAHQLPGHLTQEHDAVLSLSAYNVKLAWRDGEDIILRVPIHDIAAVSYVRDDAAHLVVLKTAQDPGISPSQSLCAESSRGLSAGSLSESAVGPVEACCLVILAAESKVAAEELCCLLGQVFQVVYTESTIDFLDRAIFDGASTPTHHLSLHSDDSSTKVDIKETYEVEASTFCFPESVDVGGASPHSKTISESELSASATELLQDYMLTLRTKLSSQEIQQFAALLHEYRNGASIHEFCINLRQLYGDSRKFLLLGLRPFIPEKDSQHFENFLETIGVKDGRGIITDSFGRHRRALSTTSSSTTNGNRATGSSDDRSAPSEGDEWDRMISDISSDIEALGCSMDQDSA
Organism_Source Homo sapiens
Functional_Classification phosphotyrosine-binding domain
Cellular_Localization Cytoplasm
Gene_Names CCM2
UniProt_ID Q9BSQ5
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name KRIT1Biotin-NPX(Y/F)3
Peptide_Sequence TNRVDKVVINPYFG
Peptide_Length 14
Peptide_SMILES CC[C@H](C)[C@H](NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](N)[C@@H](C)O)C(C)C)C(C)C)C(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Biotinylation
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 1621.86
Aliphatic_Index 90.00000
Aromaticity 0.14286
Average_Rotatable_Bonds 3.57143
Charge_at_pH_7 0.99728
Isoelectric_Point 9.29736
Number_of_Hydrogen_Bond_Acceptors 22
Number_of_Hydrogen_Bond_Donors 23
Topological_Polar_Surface_Area 684.69000
X_logP_energy -5.95803
Interaction Information
Affinity KD=15.5 uM
Affinity_Assay Bio-Layer Interferometry
PDB_ID None
Type Affinity ligand
Structure
Reference Information
Document_Type Research Articles
Title Structural basis for the disruption of the cerebral cavernous malformations 2 (CCM2)interaction with Krev interaction trapped 1 (KRIT1)by disease-associated mutations.
Release_Year 2015
PMID 25525273
DOI 10.1074/jbc.M114.616433