6SQO
Crystal structure of human MDM2 RING domain homodimer bound to UbcH5B-Ub
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043066 | biological_process | negative regulation of apoptotic process |
| A | 0051726 | biological_process | regulation of cell cycle |
| A | 0061630 | molecular_function | ubiquitin protein ligase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000209 | biological_process | protein polyubiquitination |
| B | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| B | 0016567 | biological_process | protein ubiquitination |
| B | 0016740 | molecular_function | transferase activity |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0036211 | biological_process | protein modification process |
| B | 0051865 | biological_process | protein autoubiquitination |
| B | 0061630 | molecular_function | ubiquitin protein ligase activity |
| B | 0061631 | molecular_function | ubiquitin conjugating enzyme activity |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0070936 | biological_process | protein K48-linked ubiquitination |
| D | 0005634 | cellular_component | nucleus |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0043066 | biological_process | negative regulation of apoptotic process |
| D | 0051726 | biological_process | regulation of cell cycle |
| D | 0061630 | molecular_function | ubiquitin protein ligase activity |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 501 |
| Chain | Residue |
| A | CYS438 |
| A | CYS441 |
| A | CYS461 |
| A | CYS464 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | HIS452 |
| A | HIS457 |
| A | CYS475 |
| A | CYS478 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | ILE485 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 201 |
| Chain | Residue |
| A | HOH622 |
| B | ALA2 |
| B | LEU3 |
| B | LYS4 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue NO3 B 202 |
| Chain | Residue |
| B | ARG136 |
| B | GLU140 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| D | CYS438 |
| D | CYS441 |
| D | CYS461 |
| D | CYS464 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 502 |
| Chain | Residue |
| D | HIS452 |
| D | HIS457 |
| D | CYS475 |
| D | CYS478 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue CL D 503 |
| Chain | Residue |
| D | ILE485 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue CL E 201 |
| Chain | Residue |
| E | ALA2 |
| E | LEU3 |
| E | LYS4 |
| E | HOH422 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue NO3 E 202 |
| Chain | Residue |
| E | LYS85 |
| E | ARG90 |
| E | LYS133 |
| E | ARG136 |
| E | HOH322 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 82 |
| Details | Zinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Motif: {"description":"Nucleolar localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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_FI4 |
| Number of Residues | 150 |
| Details | Domain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Interacts with activating enzyme"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Essential for function"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PINK1","evidences":[{"source":"PubMed","id":"24660806","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24751536","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24784582","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25527291","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"(Microbial infection) ADP-ribosylthreonine","evidences":[{"source":"PubMed","id":"32330457","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"ADP-ribosylglycine","evidences":[{"source":"PubMed","id":"28525742","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16443603","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15466860","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752573","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34239127","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"25752577","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16543144","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18719106","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






