3RZV
The Crystal Structure of a E280A Mutant of the Catalytic Domain of AMSH
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 | ASP309 |
A | HIS335 |
A | HIS337 |
A | ASP348 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 2 |
Chain | Residue |
A | HIS350 |
A | CYS390 |
A | HIS396 |
A | HIS398 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 |
Chain | Residue | Details |
A | HIS335 | |
A | HIS337 | |
A | ASP348 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q96FJ0 |
Chain | Residue | Details |
A | HIS350 | |
A | CYS390 | |
A | HIS396 | |
A | HIS398 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | SITE: Indirect zinc-binding => ECO:0000250|UniProtKB:Q96FJ0 |
Chain | Residue | Details |
A | ALA280 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:11483516, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER243 | |
A | SER247 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:11483516 |
Chain | Residue | Details |
A | SER245 |