Crystal structure of monoubiquitinated TRIM21 RING (Ub-RING) In complex with ubiquitin charged Ube2N (Ube2N~Ub) and Ube2V2. Determined by X-ray diffraction at 2.2 Å resolution. Released 27 Jan 2021.
Explore 7BBD in 3D Show helices and sheets RCSB PDB PDBe
7BBD contains 24 α-helices and 39 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-23 | 13 | |
| β-strand | 31-35 | 5 | 9 |
| β-strand | 45-51 | 7 | 9 |
| α-helix | 52-53 | 2 | |
| β-strand | 62-68 | 7 | 9 |
| α-helix | 77-78 | 2 | |
| β-strand | 79-82 | 4 | 9 |
| β-strand | 84 | 1 | 10 |
| β-strand | 91 | 1 | 11 |
| β-strand | 98 | 1 | 11 |
| α-helix | 104-107 | 4 | |
| α-helix | 115-125 | 11 | |
| α-helix | 129-132 | 4 | |
| α-helix | 137-138 | 2 | |
| β-strand | 142 | 1 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 1-7 | 7 | 1 |
| β-strand | 12-17 | 6 | 1 |
| β-strand | 22 | 1 | 2 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 1 |
| β-strand | 48-49 | 2 | 1 |
| β-strand | 55 | 1 | 2 |
| β-strand | 66-71 | 6 | 1 |
| α-helix | 80-89 | 10 | |
| β-strand | 91 | 1 | 3 |
| β-strand | 98 | 1 | 3 |
| β-strand | 102-104 | 3 | 4 |
| β-strand | 110-112 | 3 | 4 |
| α-helix | 113-119 | 7 | |
| β-strand | 124-126 | 3 | 5 |
| β-strand | 133-135 | 3 | 5 |
| α-helix | 136-138 | 3 | |
| β-strand | 140-141 | 2 | 4 |
| α-helix | 143-156 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| α-helix | 6-17 | 12 | |
| α-helix | 19-20 | 2 | |
| β-strand | 23-28 | 6 | 12 |
| β-strand | 31-40 | 10 | 12 |
| α-helix | 41-42 | 2 | |
| β-strand | 51-57 | 7 | 12 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-71 | 4 | 12 |
| β-strand | 77 | 1 | 13 |
| β-strand | 80 | 1 | 13 |
| β-strand | 85 | 1 | 12 |
| β-strand | 86 | 1 | 13 |
| β-strand | 88 | 1 | 8 |
| α-helix | 89-91 | 3 | |
| α-helix | 101-113 | 13 | |
| α-helix | 123-131 | 9 | |
| α-helix | 133-147 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 6 |
| β-strand | 12-16 | 5 | 6 |
| β-strand | 22 | 1 | 7 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 6 |
| β-strand | 48-49 | 2 | 6 |
| β-strand | 55 | 1 | 7 |
| β-strand | 65-71 | 7 | 6 |
| β-strand | 75 | 1 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Polyubiquitin-B,E3 ubiquitin-protein ligase TRIM21 | B | protein | 164 | Homo sapiens | P0CG47 (AlphaFold model), P19474 (AlphaFold model) |
| Polyubiquitin-C | D | protein | 76 | Homo sapiens | P0CG48 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 variant 2 | A | protein | 150 | Homo sapiens | Q15819 (AlphaFold model) |
| Ubiquitin-conjugating enzyme E2 N | C | protein | 153 | Homo sapiens | P61088 |
>7BBD_1 Polyubiquitin-B,E3 ubiquitin-protein ligase TRIM21 (chains B) GSHMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLS DYNIQKESTLHLVLRLRAAMASAARLTMMWEEVTCPICLDPFVEPVSIECGHSFCQECIS QVGKGGGSVCPVCRQRFLLKNLRPNRQLANMVNNLKEISQEARE
>7BBD_2 Polyubiquitin-C (chains D) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGG
>7BBD_3 Ubiquitin-conjugating enzyme E2 variant 2 (chains A) GSQEFMAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPR TNYENRIYSLKVECGPKYPEAPPSVRFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSI KVVLQELRRLMMSKENMKLPQPPEGQTYNN
>7BBD_4 Ubiquitin-conjugating enzyme E2 N (chains C) GMAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLP EEYPMAAPKVRFMTKIYHPNVDKLGRIKLDILADKWSPALQIRTVLLSIQALLSAPNPDD PLANDVAEQWKTNEAQAIETARAWTRLYAMNNI
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 2 |
RING domains act as both substrate and enzyme in a catalytic arrangement to drive self-anchored ubiquitination. Kiss, L., Clift, D., Renner, N. et al. Nat Commun (2021) 12:1220-1220. DOI 10.1038/s41467-021-21443-6 · PubMed
Other PDB entries of the same protein (UniProt P0CG47 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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