4JXE
Crystal structure of Schizosaccharomyces pombe sst2 catalytic domain
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 |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0016579 | biological_process | protein deubiquitination |
| B | 0061578 | molecular_function | K63-linked deubiquitinase activity |
| B | 0070536 | biological_process | protein K63-linked deubiquitination |
| B | 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 | HIS341 |
| A | HIS343 |
| A | ASP354 |
| A | HOH634 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 502 |
| Chain | Residue |
| A | HIS356 |
| A | CYS397 |
| A | HIS404 |
| A | HIS406 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 503 |
| Chain | Residue |
| A | THR319 |
| A | TYR361 |
| A | GLY318 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 504 |
| Chain | Residue |
| A | LYS426 |
| A | LEU427 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | HIS341 |
| B | HIS343 |
| B | ASP354 |
| B | HOH636 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 502 |
| Chain | Residue |
| B | HIS356 |
| B | CYS397 |
| B | HIS404 |
| B | HIS406 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 503 |
| Chain | Residue |
| B | PHE403 |
| B | HIS404 |
| B | HOH635 |
| B | HOH674 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 504 |
| Chain | Residue |
| B | VAL429 |
| B | VAL430 |
| B | ASP431 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 505 |
| Chain | Residue |
| B | GLU255 |
| B | LEU386 |
| B | PRO388 |
| B | GLU389 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 506 |
| Chain | Residue |
| B | CYS288 |
| B | CYS317 |
| B | GLY318 |
| B | THR319 |
| B | TYR361 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TRS B 507 |
| Chain | Residue |
| B | LYS249 |
| B | ARG261 |
| B | THR262 |
| B | ASN298 |
| B | HOH631 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TRS B 508 |
| Chain | Residue |
| B | HIS304 |
| B | HIS332 |
| B | GLN428 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 |
| Chain | Residue | Details |
| A | HIS341 | |
| A | HIS343 | |
| A | ASP354 | |
| B | HIS341 | |
| B | HIS343 | |
| B | ASP354 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS356 | |
| A | CYS397 | |
| A | HIS404 | |
| A | HIS406 | |
| B | HIS356 | |
| B | CYS397 | |
| B | HIS404 | |
| B | HIS406 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Indirect zinc-binding => ECO:0000250 |
| Chain | Residue | Details |
| A | GLU286 | |
| B | GLU286 |
