3RZU
The Crystal Structure 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 |
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 |
D | 0008233 | molecular_function | peptidase activity |
D | 0008237 | molecular_function | metallopeptidase activity |
D | 0016579 | biological_process | protein deubiquitination |
D | 0061578 | molecular_function | K63-linked deubiquitinase activity |
D | 0070536 | biological_process | protein K63-linked deubiquitination |
D | 0140492 | molecular_function | metal-dependent deubiquitinase activity |
E | 0008233 | molecular_function | peptidase activity |
E | 0008237 | molecular_function | metallopeptidase activity |
E | 0016579 | biological_process | protein deubiquitination |
E | 0061578 | molecular_function | K63-linked deubiquitinase activity |
E | 0070536 | biological_process | protein K63-linked deubiquitination |
E | 0140492 | molecular_function | metal-dependent deubiquitinase activity |
F | 0008233 | molecular_function | peptidase activity |
F | 0008237 | molecular_function | metallopeptidase activity |
F | 0016579 | biological_process | protein deubiquitination |
F | 0061578 | molecular_function | K63-linked deubiquitinase activity |
F | 0070536 | biological_process | protein K63-linked deubiquitination |
F | 0140492 | molecular_function | metal-dependent deubiquitinase activity |
G | 0008233 | molecular_function | peptidase activity |
G | 0008237 | molecular_function | metallopeptidase activity |
G | 0016579 | biological_process | protein deubiquitination |
G | 0061578 | molecular_function | K63-linked deubiquitinase activity |
G | 0070536 | biological_process | protein K63-linked deubiquitination |
G | 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 | HOH14 |
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 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 3 |
Chain | Residue |
B | HIS337 |
B | ASP348 |
B | HIS335 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 4 |
Chain | Residue |
B | HIS350 |
B | CYS390 |
B | HIS396 |
B | HIS398 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 5 |
Chain | Residue |
C | HOH134 |
C | HIS335 |
C | HIS337 |
C | ASP348 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN C 6 |
Chain | Residue |
C | HIS350 |
C | CYS390 |
C | HIS396 |
C | HIS398 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN D 7 |
Chain | Residue |
D | HIS335 |
D | HIS337 |
D | ASP348 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 8 |
Chain | Residue |
D | HOH136 |
D | HIS350 |
D | CYS390 |
D | HIS396 |
D | HIS398 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN E 9 |
Chain | Residue |
E | HOH135 |
E | HIS335 |
E | HIS337 |
E | ASP348 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN E 10 |
Chain | Residue |
E | HOH103 |
E | HIS350 |
E | CYS390 |
E | HIS396 |
E | HIS398 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 11 |
Chain | Residue |
F | HOH155 |
F | HIS335 |
F | HIS337 |
F | ASP348 |
site_id | BC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN F 12 |
Chain | Residue |
F | HIS350 |
F | CYS390 |
F | HIS396 |
F | HIS398 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN G 13 |
Chain | Residue |
G | HOH138 |
G | HIS335 |
G | HIS337 |
G | ASP348 |
site_id | BC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN G 14 |
Chain | Residue |
G | HOH79 |
G | HIS350 |
G | CYS390 |
G | HIS396 |
G | HIS398 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 21 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01182 |
Chain | Residue | Details |
A | HIS335 | |
D | HIS335 | |
D | HIS337 | |
D | ASP348 | |
E | HIS335 | |
E | HIS337 | |
E | ASP348 | |
F | HIS335 | |
F | HIS337 | |
F | ASP348 | |
G | HIS335 | |
A | HIS337 | |
G | HIS337 | |
G | ASP348 | |
A | ASP348 | |
B | HIS335 | |
B | HIS337 | |
B | ASP348 | |
C | HIS335 | |
C | HIS337 | |
C | ASP348 |
site_id | SWS_FT_FI2 |
Number of Residues | 28 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q96FJ0 |
Chain | Residue | Details |
A | HIS350 | |
C | CYS390 | |
C | HIS396 | |
C | HIS398 | |
D | HIS350 | |
D | CYS390 | |
D | HIS396 | |
D | HIS398 | |
E | HIS350 | |
E | CYS390 | |
E | HIS396 | |
A | CYS390 | |
E | HIS398 | |
F | HIS350 | |
F | CYS390 | |
F | HIS396 | |
F | HIS398 | |
G | HIS350 | |
G | CYS390 | |
G | HIS396 | |
G | HIS398 | |
A | HIS396 | |
A | HIS398 | |
B | HIS350 | |
B | CYS390 | |
B | HIS396 | |
B | HIS398 | |
C | HIS350 |
site_id | SWS_FT_FI3 |
Number of Residues | 7 |
Details | SITE: Indirect zinc-binding => ECO:0000250|UniProtKB:Q96FJ0 |
Chain | Residue | Details |
A | GLU280 | |
B | GLU280 | |
C | GLU280 | |
D | GLU280 | |
E | GLU280 | |
F | GLU280 | |
G | GLU280 |
site_id | SWS_FT_FI4 |
Number of Residues | 14 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:11483516, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER243 | |
E | SER247 | |
F | SER243 | |
F | SER247 | |
G | SER243 | |
G | SER247 | |
A | SER247 | |
B | SER243 | |
B | SER247 | |
C | SER243 | |
C | SER247 | |
D | SER243 | |
D | SER247 | |
E | SER243 |
site_id | SWS_FT_FI5 |
Number of Residues | 7 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:11483516 |
Chain | Residue | Details |
A | SER245 | |
B | SER245 | |
C | SER245 | |
D | SER245 | |
E | SER245 | |
F | SER245 | |
G | SER245 |