5D1M
Crystal Structure of UbcH5B in Complex with the RING-U5BR Fragment of AO7 (P199A)
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000151 | cellular_component | ubiquitin ligase complex |
A | 0000209 | biological_process | protein polyubiquitination |
A | 0004842 | molecular_function | ubiquitin-protein transferase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
A | 0016567 | biological_process | protein ubiquitination |
A | 0016740 | molecular_function | transferase activity |
A | 0019787 | molecular_function | ubiquitin-like protein transferase activity |
A | 0031625 | molecular_function | ubiquitin protein ligase binding |
A | 0032991 | cellular_component | protein-containing complex |
A | 0036211 | biological_process | protein modification process |
A | 0051865 | biological_process | protein autoubiquitination |
A | 0061630 | molecular_function | ubiquitin protein ligase activity |
A | 0061631 | molecular_function | ubiquitin conjugating enzyme activity |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070936 | biological_process | protein K48-linked ubiquitination |
B | 0061630 | molecular_function | ubiquitin protein ligase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue OXL A 201 |
Chain | Residue |
A | GLU140 |
A | TRP141 |
A | LYS144 |
A | TYR145 |
A | PEG202 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue PEG A 202 |
Chain | Residue |
A | OXL201 |
A | HOH397 |
A | ARG72 |
A | SER80 |
A | TRP141 |
A | TYR145 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue ZN B 301 |
Chain | Residue |
B | CYS135 |
B | CYS138 |
B | HIS158 |
B | CYS161 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue ZN B 302 |
Chain | Residue |
B | CYS153 |
B | HIS155 |
B | CYS198 |
B | CYS201 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | THR149 |
B | LYS150 |
B | THR151 |
B | PRO152 |
B | VAL206 |
B | GLU247 |
B | ARG248 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue EDO B 304 |
Chain | Residue |
A | ASN41 |
A | GLN46 |
A | MET147 |
B | LYS150 |
B | TYR154 |
B | ARG248 |
Functional Information from PROSITE/UniProt
site_id | PS00183 |
Number of Residues | 16 |
Details | UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL |
Chain | Residue | Details |
A | TYR74-LEU89 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 67 |
Details | ZN_FING: RING-type => ECO:0000255|PROSITE-ProRule:PRU00175 |
Chain | Residue | Details |
B | CYS135-ARG202 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26475854, ECO:0007744|PDB:5D1K, ECO:0007744|PDB:5D1L, ECO:0007744|PDB:5D1M |
Chain | Residue | Details |
B | CYS135 | |
B | CYS138 | |
B | CYS153 | |
B | HIS155 | |
B | HIS158 | |
B | CYS161 | |
B | CYS198 | |
B | CYS201 |