PPIST05324

Protein Information
Protein_Chain B
Protein_Sequence IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRLGEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRVASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKSAYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQKNKPGVYTKVCNYVSWIKQTIASN
Peptide Information
Peptide_Chain A
Peptide_Sequence EQECEPGQTKKQDCNTCRCGSDGVWACTRMGCPPHA
Peptide_Length 36
Non-standard residues No
Interaction Information
PDB_ID 2XTT
Method X-RAY DIFFRACTION
Resolution 0.93 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 The catalytic aspartate is protonated in the Michaelis complex formed between trypsin and an in vitro evolved substrate-like inhibitor: a refined mechanism of serine protease action.
Release_Year 2011
PMID 21097875
DOI 10.1074/jbc.M110.161604