5VF0: Human RAD18

Solution NMR structure of human RAD18 (198-240) in complex with ubiquitin. Determined by solution NMR. Released 17 May 2017.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
943
Mol. weight
13.87 kDa
Ligands
ZN
Released
17 May 2017

Explore 5VF0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5VF0 contains 4 α-helices and 9 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: 2 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand2-761
β-strand12-1651
β-strand2212
α-helix23-3412
β-strand41-4551
β-strand48-4921
β-strand5512
α-helix57-593
β-strand66-7161
Chain B: 2 helices, 2 β-strands
ElementResiduesLengthSheet
β-strand201-20223
β-strand211-21223
α-helix216-23015
α-helix232-2332

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Polyubiquitin-BAprotein76Homo sapiensP0CG47 (AlphaFold model)
E3 ubiquitin-protein ligase RAD18Bprotein46Homo sapiensQ9NS91 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5VF0_1 Polyubiquitin-B (chains A)
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN
IQKESTLHLVLRLRGG
Sequence of entity 2 (B), FASTA
>5VF0_2 E3 ubiquitin-protein ligase RAD18 (chains B)
GHMQVTKVDCPVCGVNIPESHINKHLDSCLSREEKKESLRSSVHKR

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Primary citation

Mechanisms of Ubiquitin-Nucleosome Recognition and Regulation of 53BP1 Chromatin Recruitment by RNF168/169 and RAD18. Hu, Q., Botuyan, M.V., Cui, G. et al. Mol Cell (2017) 66:473-487.e9. DOI 10.1016/j.molcel.2017.04.009 · 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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