1UD7
SOLUTION STRUCTURE OF THE DESIGNED HYDROPHOBIC CORE MUTANT OF UBIQUITIN, 1D7
Functional Information from PROSITE/UniProt
site_id | PS00299 |
Number of Residues | 26 |
Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
Chain | Residue | Details |
A | LYS27-ASP52 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | SITE: Interacts with activating enzyme |
Chain | Residue | Details |
A | THR14 | |
A | ASP32 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Essential for function |
Chain | Residue | Details |
A | ALA28 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 |
Chain | Residue | Details |
A | LEU8 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) |
Chain | Residue | Details |
A | ILE36 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 |
Chain | Residue | Details |
A | VAL23 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 |
Chain | Residue | Details |
A | ASN25 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 |
Chain | Residue | Details |
A | PHE26 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742 |
Chain | Residue | Details |
A | ILE36 |