PPIST14337

Protein Information
Protein_Chain A[auth B]; B[auth E]; C[auth H]/D[auth A]; E[auth D]; F[auth G]
Protein_Sequence GSQEFMAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSVRFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQTYNN/GMAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNVDKLGRIKLDILADKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI
Peptide Information
Peptide_Chain G[auth C]; H[auth F]; I
Peptide_Sequence MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGG
Peptide_Length 76
Non-standard residues No
Interaction Information
PDB_ID 7BBF
Method X-RAY DIFFRACTION
Resolution 2.54 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 RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination.
Release_Year 2021
PMID 33619271
DOI 10.1038/s41467-021-21443-6