2ZNR
Crystal structure of the DUB domain of human AMSH-LP
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 1 |
Chain | Residue |
A | HIS362 |
A | CYS402 |
A | HIS408 |
A | HIS410 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 2 |
Chain | Residue |
A | HIS347 |
A | HIS349 |
A | ASP360 |
A | HOH517 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PR A 437 |
Chain | Residue |
A | ASP427 |
A | HOH705 |
A | HOH706 |
A | HOH707 |
A | HOH708 |
A | ASP274 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 438 |
Chain | Residue |
A | TYR322 |
A | ASP324 |
A | LYS429 |
A | HOH454 |
A | HOH538 |
A | HOH630 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 439 |
Chain | Residue |
A | LEU271 |
A | PRO272 |
A | GLU273 |
A | LEU275 |
A | CYS276 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 3 |
Chain | Residue |
A | CYS420 |
A | VAL423 |
A | HOH469 |
A | HOH470 |
A | HOH557 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 4 |
Chain | Residue |
A | HIS262 |
A | GLU264 |
A | THR307 |
A | HOH458 |
A | HOH490 |
A | HOH536 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 5 |
Chain | Residue |
A | ARG267 |
A | ASN304 |
A | LEU369 |
A | HOH477 |
A | HOH656 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 6 |
Chain | Residue |
A | GLU284 |
A | GLU305 |
A | HOH606 |
A | HOH655 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 7 |
Chain | Residue |
A | LYS315 |
A | PRO409 |
A | ARG436 |
A | HOH519 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 128 |
Details | Domain: {"description":"MPN","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 13 |
Details | Motif: {"description":"JAMM motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01182","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18758443","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZNR","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"18758443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34425109","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2ZNR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7L97","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Site: {"description":"Indirect zinc-binding","evidences":[{"source":"PubMed","id":"18758443","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |