Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008233 | molecular_function | peptidase activity |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0016579 | biological_process | protein deubiquitination |
A | 0061578 | molecular_function | K63-linked deubiquitinase activity |
A | 0070536 | biological_process | protein K63-linked deubiquitination |
A | 0140492 | molecular_function | metal-dependent deubiquitinase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 501 |
Chain | Residue |
A | HIS356 |
A | CYS397 |
A | HIS404 |
A | HIS406 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO A 502 |
Chain | Residue |
B | LEU71 |
B | EDO101 |
A | LEU325 |
A | GLN329 |
A | THR336 |
A | TYR361 |
B | LEU8 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | ASN284 |
A | SER314 |
A | ASP315 |
A | THR345 |
A | HOH622 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
Chain | Residue |
A | THR316 |
A | CYS317 |
A | GLY318 |
B | THR22 |
B | GLY53 |
B | ARG74 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | GLY381 |
A | ILE382 |
A | MET413 |
A | VAL414 |
A | GLN416 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | LYS258 |
A | GLN362 |
A | PRO366 |
A | ASP387 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 101 |
Chain | Residue |
A | EDO502 |
B | THR7 |
B | LEU8 |
B | LEU69 |
B | VAL70 |
B | LEU71 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO C 101 |
Chain | Residue |
A | PHE349 |
C | GLN62 |
C | LYS63 |
C | GLU64 |
C | SER65 |
Functional Information from PROSITE/UniProt
site_id | PS00299 |
Number of Residues | 26 |
Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
Chain | Residue | Details |
B | LYS27-ASP52 | |
C | LYS27-ASP52 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 130 |
Details | Domain: {"description":"MPN","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 13 |
Details | Motif: {"description":"JAMM motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Site: {"description":"Indirect zinc-binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 75 |
Details | Domain: {"description":"Ubiquitin-like 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |