PPIST12675

Protein Information
Protein_Chain B/A
Protein_Sequence MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDWSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM/GSHSMRYFDTAMSRPGRGEPRFISVGYVDDTQFVRFDSDAASPREEPRAPWIEQEGPEYWDRNTQIFKTNTQTDRCSLRNLRGYYNQSEAGSHTLQSMYGCDVGPDGRLLRGHNQYAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAARVAEQDRAYLEGTCVEWLRRYLENGKDTLERADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
Peptide Information
Peptide_Chain C
Peptide_Sequence RARARAAAKKGYCL
Peptide_Length 14
Non-standard residues No
Interaction Information
PDB_ID 6P2F
Method X-RAY DIFFRACTION
Resolution 1.48 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 ERAP1 enzyme-mediated trimming and structural analyses of MHC I-bound precursor peptides yield novel insights into antigen processing and presentation.
Release_Year 2019
PMID 31601650
DOI 10.1074/jbc.RA119.010102