3IHP
Covalent Ubiquitin-Usp5 Complex
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
A | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005764 | cellular_component | lysosome |
A | 0005829 | cellular_component | cytosol |
A | 0006508 | biological_process | proteolysis |
A | 0008233 | molecular_function | peptidase activity |
A | 0008234 | molecular_function | cysteine-type peptidase activity |
A | 0008270 | molecular_function | zinc ion binding |
A | 0016567 | biological_process | protein ubiquitination |
A | 0016579 | biological_process | protein deubiquitination |
A | 0032436 | biological_process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
A | 0043130 | molecular_function | ubiquitin binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0071108 | biological_process | protein K48-linked deubiquitination |
A | 0098793 | cellular_component | presynapse |
A | 0101005 | molecular_function | deubiquitinase activity |
A | 0140251 | biological_process | regulation protein catabolic process at presynapse |
A | 2000059 | biological_process | negative regulation of ubiquitin-dependent protein catabolic process |
B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
B | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005764 | cellular_component | lysosome |
B | 0005829 | cellular_component | cytosol |
B | 0006508 | biological_process | proteolysis |
B | 0008233 | molecular_function | peptidase activity |
B | 0008234 | molecular_function | cysteine-type peptidase activity |
B | 0008270 | molecular_function | zinc ion binding |
B | 0016567 | biological_process | protein ubiquitination |
B | 0016579 | biological_process | protein deubiquitination |
B | 0032436 | biological_process | positive regulation of proteasomal ubiquitin-dependent protein catabolic process |
B | 0043130 | molecular_function | ubiquitin binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0071108 | biological_process | protein K48-linked deubiquitination |
B | 0098793 | cellular_component | presynapse |
B | 0101005 | molecular_function | deubiquitinase activity |
B | 0140251 | biological_process | regulation protein catabolic process at presynapse |
B | 2000059 | biological_process | negative regulation of ubiquitin-dependent protein catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NEH C 76 |
Chain | Residue |
A | ASN333 |
A | CYS335 |
A | GLN433 |
A | GLY794 |
C | GLY75 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NEH D 76 |
Chain | Residue |
D | GLY75 |
B | ASN333 |
B | CYS335 |
B | GLN433 |
B | GLY794 |
site_id | AC3 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE CL D 77 |
Chain | Residue |
D | ARG74 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 836 |
Chain | Residue |
A | CYS199 |
A | CYS202 |
A | CYS219 |
A | HIS232 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 836 |
Chain | Residue |
B | CYS199 |
B | CYS202 |
B | CYS219 |
B | HIS232 |
Functional Information from PROSITE/UniProt
site_id | PS00299 |
Number of Residues | 26 |
Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
Chain | Residue | Details |
C | LYS27-ASP52 |
site_id | PS00972 |
Number of Residues | 16 |
Details | USP_1 Ubiquitin specific protease (USP) domain signature 1. GIrnlGNsCYLNSvVQ |
Chain | Residue | Details |
A | GLY327-GLN342 |
site_id | PS00973 |
Number of Residues | 19 |
Details | USP_2 Ubiquitin specific protease (USP) domain signature 2. YqLfAFisHmGtstmc.GHY |
Chain | Residue | Details |
A | TYR778-TYR796 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 216 |
Details | ZN_FING: UBP-type; degenerate => ECO:0000255|PROSITE-ProRule:PRU00502 |
Chain | Residue | Details |
A | GLN175-MET283 | |
B | GLN175-MET283 | |
D | ARG54 | |
D | ARG72 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
A | CYS335 | |
B | CYS335 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093 |
Chain | Residue | Details |
A | GLU818 | |
B | GLU818 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00502 |
Chain | Residue | Details |
A | CYS199 | |
A | CYS202 | |
A | CYS219 | |
A | HIS232 | |
B | CYS199 | |
B | CYS202 | |
B | CYS219 | |
B | HIS232 |
site_id | SWS_FT_FI5 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | TRP209 | |
B | ASP264 | |
A | ARG221 | |
A | TYR259 | |
A | TYR261 | |
A | ASP264 | |
B | TRP209 | |
B | ARG221 | |
B | TYR259 | |
B | TYR261 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
A | ALA2 | |
B | ALA2 | |
D | LYS63 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER156 | |
B | SER156 | |
D | LYS11 | |
D | LYS48 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR292 | |
B | THR292 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P56399 |
Chain | Residue | Details |
A | THR623 | |
B | THR623 |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | GLN779 | |
A | SER785 | |
B | GLN779 | |
B | SER785 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | PHE783 | |
B | PHE783 |