7OYF
Crystal structure of depupylase Dop in complex with Pup and ADP/trifluoromagnesate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0008233 | molecular_function | peptidase activity |
A | 0010498 | biological_process | proteasomal protein catabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
A | 0019941 | biological_process | modification-dependent protein catabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 0070490 | biological_process | protein pupylation |
B | 0010498 | biological_process | proteasomal protein catabolic process |
B | 0019941 | biological_process | modification-dependent protein catabolic process |
B | 0031386 | molecular_function | protein tag activity |
B | 0070490 | biological_process | protein pupylation |
B | 0070628 | molecular_function | proteasome binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | CROSSLNK: Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-? in acceptor proteins) => ECO:0000255|HAMAP-Rule:MF_02106 |
Chain | Residue | Details |
B | GLU71 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22910360 |
Chain | Residue | Details |
A | GLU8 | |
A | TYR92 | |
A | GLU99 | |
A | SER101 | |
A | HIS155 | |
A | ASN157 | |
A | ARG239 | |
A | HIS241 |