8Q7R
Ubiquitin ligation to substrate by a cullin-RING E3 ligase & Cdc34: NEDD8-CUL2-RBX1-ELOB/C-FEM1C with trapped UBE2R2~donor UB-Sil1 peptide
Summary for 8Q7R
Entry DOI | 10.2210/pdb8q7r/pdb |
EMDB information | 18207 18230 |
Descriptor | Cullin-2, ZINC ION, Protein fem-1 homolog C, ... (10 entities in total) |
Functional Keywords | cul2, fem1c, elobc, sil1, ubiquitin, ubiquitin ligase, ubiquitylation, monoubiquitylation, ligase, elongin b, elongin c |
Biological source | Homo sapiens (human) More |
Total number of polymer chains | 8 |
Total formula weight | 300667.34 |
Authors | Liwocha, J.,Prabu, J.R.,Kleiger, G.,Schulman, B.A. (deposition date: 2023-08-16, release date: 2024-02-21, Last modification date: 2024-04-24) |
Primary citation | Li, J.,Purser, N.,Liwocha, J.,Scott, D.C.,Byers, H.A.,Steigenberger, B.,Hill, S.,Tripathi-Giesgen, I.,Hinkle, T.,Hansen, F.M.,Prabu, J.R.,Radhakrishnan, S.K.,Kirkpatrick, D.S.,Reichermeier, K.M.,Schulman, B.A.,Kleiger, G. Cullin-RING ligases employ geometrically optimized catalytic partners for substrate targeting. Mol.Cell, 84:1304-, 2024 Cited by PubMed: 38382526DOI: 10.1016/j.molcel.2024.01.022 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.71 Å) |
Structure validation
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