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 |
C | 0008233 | molecular_function | peptidase activity |
C | 0008237 | molecular_function | metallopeptidase activity |
C | 0016579 | biological_process | protein deubiquitination |
C | 0061578 | molecular_function | K63-linked deubiquitinase activity |
C | 0070536 | biological_process | protein K63-linked deubiquitination |
C | 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 | HIS304 |
A | HIS332 |
A | CL504 |
C | GLU327 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 502 |
Chain | Residue |
A | HIS341 |
A | HIS343 |
A | ASP354 |
B | GLY76 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 503 |
Chain | Residue |
A | CYS397 |
A | HIS404 |
A | HIS406 |
A | HIS356 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL A 504 |
Chain | Residue |
A | HIS304 |
A | HIS332 |
A | GLN428 |
A | ZN501 |
C | GLU327 |
C | PHE328 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | GLN329 |
A | ASN333 |
A | LEU334 |
A | LEU335 |
B | LEU8 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 506 |
Chain | Residue |
A | GLN346 |
A | PHE349 |
A | HOH700 |
A | HOH701 |
A | HOH710 |
B | GLY76 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 507 |
Chain | Residue |
A | THR345 |
A | SER376 |
A | LYS377 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 508 |
Chain | Residue |
A | LYS270 |
A | SER380 |
A | GLY381 |
A | ILE382 |
A | GLN416 |
A | GLU422 |
site_id | AC9 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE EDO A 509 |
Chain | Residue |
A | LYS294 |
A | ARG296 |
site_id | BC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 101 |
Chain | Residue |
A | HOH633 |
B | THR7 |
B | LEU8 |
B | LEU69 |
B | VAL70 |
B | LEU71 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 501 |
Chain | Residue |
C | HIS341 |
C | HIS343 |
C | ASP354 |
D | GLY76 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 502 |
Chain | Residue |
C | HIS356 |
C | CYS397 |
C | HIS404 |
C | HIS406 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 503 |
Chain | Residue |
A | GLU327 |
C | HIS304 |
C | HIS332 |
C | CL504 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL C 504 |
Chain | Residue |
A | GLU327 |
A | PHE328 |
C | HIS304 |
C | HIS332 |
C | GLN428 |
C | ZN503 |
site_id | BC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE EDO C 505 |
Chain | Residue |
A | GLU311 |
A | THR316 |
A | CYS317 |
A | GLY318 |
A | HOH649 |
B | ARG74 |
B | HOH205 |
C | THR313 |
C | ASP315 |
site_id | BC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO C 506 |
Chain | Residue |
C | ASN333 |
C | LEU334 |
C | HOH682 |
C | HOH683 |
D | LEU8 |
D | HOH219 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE EDO C 507 |
Chain | Residue |
C | SER352 |
C | VAL353 |
C | HIS356 |
C | GLY401 |
C | LEU402 |
C | HIS404 |
C | HOH658 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO D 101 |
Chain | Residue |
C | HOH631 |
D | THR7 |
D | LEU8 |
D | LEU69 |
D | VAL70 |
D | LEU71 |
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 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 260 |
Details | Domain: {"description":"MPN","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 26 |
Details | Motif: {"description":"JAMM motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | Site: {"description":"Indirect zinc-binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 150 |
Details | Domain: {"description":"Ubiquitin-like 9","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |