2YBF: Ubiquitin-conjugating enzyme E2 B

Complex of Rad18 (Rad6 binding domain) with Rad6b. Determined by X-ray diffraction at 2.0 Å resolution. Released 20 Apr 2011.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
HOMO SAPIENS
Chains
2
Atoms
1,532
Mol. weight
20.84 kDa
Released
20 Apr 2011

Explore 2YBF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2YBF contains 10 α-helices and 7 β-strands across 2 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.

Chain A: 8 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix4-1815
α-helix20-212
β-strand24-2961
β-strand32-41101
α-helix42-432
β-strand52-5871
α-helix67-682
β-strand69-7241
β-strand8112
β-strand8611
β-strand8712
α-helix90-923
α-helix102-11413
α-helix124-1318
α-helix134-14714
Chain B: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix342-3454
α-helix347-35812

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ubiquitin-conjugating enzyme E2 BAprotein152HOMO SAPIENSP63146 (AlphaFold model)
E3 ubiquitin-protein ligase RAD18Bprotein27HOMO SAPIENSQ9NS91 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2YBF_1 UBIQUITIN-CONJUGATING ENZYME E2 B (chains A)
MSTPARRRLMRDFKRLQEDPPVGVSGAPSENNIMQWNAVIFGPEGTPFEDGTFKLVIEFS
EEYPNKPPTVRFLSKMFHPNVYADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNS
PANSQAAQLYQENKREYEKRVSAIVEQSWNDS
Sequence of entity 2 (B), FASTA
>2YBF_2 E3 UBIQUITIN-PROTEIN LIGASE RAD18 (chains B)
SKYRKKHKSEFQLLVDQARKGYKKIAG

Primary citation

E3 Ligase Rad18 Promotes Monoubiquitination Rather Than Ubiquitin Chain Formation by E2 Enzyme Rad6. Hibbert, R.G., Huang, A., Boelens, R. et al. Proc Natl Acad Sci U S A (2011) 108:5590. DOI 10.1073/PNAS.1017516108 · PubMed

Other PDB entries of the same protein (UniProt P63146 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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