PPIST11457

Protein Information
Protein_Chain A;C
Protein_Sequence MSSIQGFLADVEVHGSSRLTRTHTLRYNVRAHSLEGSEKTQLLVLIYVDEELFLKYNGDSRETEPLGCWIKGHGGNETCARETNNLLKVEEKLRGMMAEVINQKSQEEGLHTLQATLGCELLSNGSTRGFWHLGYDGQNFLTFDQKTLTWTVDGPSTQQNKMFWKTHAPRADLVKTFLDDICPAHLQRYLASLRNGLQDTGPPMVTVTCRNYPVGRVTLTCRAFNLYTREATLVWLQDGKPVQQKTFRSETILPSGDGTYQARVSIRVLPGQEPQFSCNLRHGNHSIMQTAV
Peptide Information
Peptide_Chain B;D
Peptide_Sequence MIQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDWSFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDRDM
Peptide_Length 100
Non-standard residues No
Interaction Information
PDB_ID 6A97
Method X-RAY DIFFRACTION
Resolution 2.15 angstrom
Structure
Protein-peptide residue interaction
Residues
Acidic
Polar
Basic
Aliphatic
Aromatic
Interactions
HBond
WaterBridge
Hydrophobic
SaltBridge
PiStack
PiCation
Halogen
Metal
Interaction_xlsx Download interaction table (.xlsx)
Reference Information
Title Structure of MHC class I-like MILL2 reveals heparan-sulfate binding and interdomain flexibility.
Release_Year 2018
PMID 30337538
DOI 10.1038/s41467-018-06797-8