5MNJ
Structure of MDM2-MDMX-UbcH5B-ubiquitin complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 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 |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0061630 | molecular_function | ubiquitin protein ligase activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0043066 | biological_process | negative regulation of apoptotic process |
| D | 0051726 | biological_process | regulation of cell cycle |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0000209 | biological_process | protein polyubiquitination |
| E | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005654 | cellular_component | nucleoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| E | 0016567 | biological_process | protein ubiquitination |
| E | 0016740 | molecular_function | transferase activity |
| E | 0032991 | cellular_component | protein-containing complex |
| E | 0036211 | biological_process | protein modification process |
| E | 0051865 | biological_process | protein autoubiquitination |
| E | 0061630 | molecular_function | ubiquitin protein ligase activity |
| E | 0061631 | molecular_function | ubiquitin conjugating enzyme activity |
| E | 0070062 | cellular_component | extracellular exosome |
| E | 0070936 | biological_process | protein K48-linked ubiquitination |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0061630 | molecular_function | ubiquitin protein ligase activity |
| H | 0005634 | cellular_component | nucleus |
| H | 0043066 | biological_process | negative regulation of apoptotic process |
| H | 0051726 | biological_process | regulation of cell cycle |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 501 |
| Chain | Residue |
| C | CYS438 |
| C | CYS441 |
| C | CYS461 |
| C | CYS464 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN C 502 |
| Chain | Residue |
| C | HIS452 |
| C | HIS457 |
| C | CYS475 |
| C | CYS478 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| D | CYS440 |
| D | CYS460 |
| D | CYS463 |
| D | CYS437 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 502 |
| Chain | Residue |
| D | HIS451 |
| D | HIS456 |
| D | CYS474 |
| D | CYS477 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 503 |
| Chain | Residue |
| D | ALA472 |
| D | SER473 |
| D | LYS478 |
| E | ARG139 |
| H | ALA472 |
| H | SER473 |
| H | LYS478 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN G 501 |
| Chain | Residue |
| G | CYS438 |
| G | CYS441 |
| G | CYS461 |
| G | CYS464 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN G 502 |
| Chain | Residue |
| G | HIS452 |
| G | HIS457 |
| G | CYS475 |
| G | CYS478 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue ZN H 501 |
| Chain | Residue |
| H | HIS451 |
| H | HIS456 |
| H | CYS474 |
| H | CYS477 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue ZN H 502 |
| Chain | Residue |
| H | CYS437 |
| H | CYS440 |
| H | CYS460 |
| H | CYS463 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 H 503 |
| Chain | Residue |
| D | LYS442 |
| D | ARG443 |
| D | ARG466 |
| H | LYS442 |
| H | ARG443 |
| H | ARG466 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide GLY F 76 and LYS E 85 |
| Chain | Residue |
| E | HIS75 |
| E | ASN77 |
| E | ILE78 |
| E | ILE84 |
| E | LEU86 |
| E | ASP117 |
| E | LEU119 |
| E | VAL120 |
| E | TYR134 |
| F | GLY75 |
Functional Information from PROSITE/UniProt
| site_id | PS00299 |
| Number of Residues | 26 |
| Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
| Chain | Residue | Details |
| B | LYS27-ASP52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 75 |
| Details | Domain: {"description":"Ubiquitin-like 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 164 |
| Details | Zinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Motif: {"description":"Nucleolar localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by ATM","evidences":[{"source":"PubMed","id":"19816404","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Motif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |






