6M2C
Distinct mechanism of MUL1-RING domain simultaneously recruiting E2 enzyme and the substrate p53-TAD domain
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B, C, D (A, B, C, D) | Ubiquitin-conjugating enzyme E2 D2 | polymer | 149 | 16899.4 | 4 | UniProt (P62837) Pfam (PF00179) | Homo sapiens (Human) | (E3-independent) E2 ubiquitin-conjugating enzyme D2,E2 ubiquitin-conjugating enzyme D2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2(17)KB 2,Ubiquitin-conjugating enzyme E2-17 kDa 2,Ubiquitin-protein ligase D2,p53-regulated ubiquitin-conjugating enzyme 1 |
| 2 | E, F, G, H (E, F, G, H) | Mitochondrial ubiquitin ligase activator of NFKB 1 | polymer | 55 | 6107.4 | 4 | UniProt (Q969V5) Pfam (PF13920) | Homo sapiens (Human) | E3 SUMO-protein ligase MUL1,E3 ubiquitin-protein ligase MUL1,Growth inhibition and death E3 ligase,Mitochondrial-anchored protein ligase,MAPL,Putative NF-kappa-B-activating protein 266,RING finger protein 218,RING-type E3 ubiquitin transferase NFKB 1 |
| 3 | I, J, K, L, M... (E, F, G, H) | ZINC ION | non-polymer | 65.4 | 8 | Chemie (ZN) | |||
| 4 | Q, R, S, T, U... (A, B, C, D, E...) | water | water | 18.0 | 62 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 1 - 147 (UniProt: P62837)
| PDB | External Database | Details |
|---|---|---|
| Gly -1 | - | expression tag |
| Ser 0 | - | expression tag |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 8 |
| Total formula weight | 92026.8 | |
| Non-Polymers* | Number of molecules | 8 |
| Total formula weight | 523.3 | |
| All* | Total formula weight | 92550.1 |
