4MSJ
Crystal structure of S. pombe AMSH-like protease SST2 catalytic domain from P212121 space group
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 |
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 | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 501 |
Chain | Residue |
A | CYS288 |
A | GLY318 |
A | THR319 |
A | THR357 |
A | TYR361 |
A | HOH646 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 502 |
Chain | Residue |
A | PO4507 |
A | HOH617 |
A | LYS409 |
A | TYR411 |
A | PO4506 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 503 |
Chain | Residue |
A | PRO388 |
A | GLN392 |
A | HOH724 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE EDO A 504 |
Chain | Residue |
A | THR316 |
A | GLY318 |
A | LEU402 |
A | GLY508 |
A | HOH703 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 505 |
Chain | Residue |
A | ARG433 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE PO4 A 506 |
Chain | Residue |
A | LYS409 |
A | EDO502 |
A | PO4507 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 A 507 |
Chain | Residue |
A | LYS294 |
A | LYS409 |
A | THR412 |
A | MET413 |
A | EDO502 |
A | PO4506 |
A | HOH652 |
A | HOH671 |
A | HOH710 |
A | HOH728 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GLY A 508 |
Chain | Residue |
A | GLU407 |
A | EDO504 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 509 |
Chain | Residue |
A | HIS341 |
A | HIS343 |
A | ASP354 |
A | HOH633 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 510 |
Chain | Residue |
A | HIS356 |
A | CYS397 |
A | HIS404 |
A | HIS406 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 501 |
Chain | Residue |
B | GLY318 |
B | THR319 |
B | TYR361 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO B 502 |
Chain | Residue |
B | ALA415 |
B | GLN416 |
B | HOH639 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 503 |
Chain | Residue |
B | HIS341 |
B | HIS343 |
B | ASP354 |
B | HOH612 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 504 |
Chain | Residue |
B | HIS356 |
B | CYS397 |
B | HIS404 |
B | HIS406 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO C 501 |
Chain | Residue |
C | GLY318 |
C | THR319 |
C | TYR361 |
site_id | BC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PO4 C 502 |
Chain | Residue |
B | LYS396 |
C | HIS251 |
site_id | BC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 503 |
Chain | Residue |
C | HIS341 |
C | HIS343 |
C | ASP354 |
C | HOH601 |
site_id | BC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 504 |
Chain | Residue |
C | HIS356 |
C | CYS397 |
C | HIS404 |
C | HIS406 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 |
Chain | Residue | Details |
A | HIS341 | |
A | HIS343 | |
A | ASP354 | |
B | HIS341 | |
B | HIS343 | |
B | ASP354 | |
C | HIS341 | |
C | HIS343 | |
C | ASP354 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | HIS356 | |
C | CYS397 | |
C | HIS404 | |
C | HIS406 | |
A | CYS397 | |
A | HIS404 | |
A | HIS406 | |
B | HIS356 | |
B | CYS397 | |
B | HIS404 | |
B | HIS406 | |
C | HIS356 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | SITE: Indirect zinc-binding => ECO:0000250 |
Chain | Residue | Details |
A | GLU286 | |
B | GLU286 | |
C | GLU286 |