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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 DOI10.2210/pdb8q7r/pdb
EMDB information18207 18230
DescriptorCullin-2, ZINC ION, Protein fem-1 homolog C, ... (10 entities in total)
Functional Keywordscul2, fem1c, elobc, sil1, ubiquitin, ubiquitin ligase, ubiquitylation, monoubiquitylation, ligase, elongin b, elongin c
Biological sourceHomo sapiens (human)
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Total number of polymer chains8
Total formula weight300667.34
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 citationLi, 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: 38382526
DOI: 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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