Solution structure of the tandem UIMs of RAP80. Determined by solution NMR. Released 19 Mar 2014.
Explore 2MKG in 3D Show helices and sheets RCSB PDB PDBe
2MKG contains 5 α-helices and 0 β-strands across 1 chain. 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 | -3--1 | 3 | |
| α-helix | 0-80 | 8 | |
| α-helix | 81-97 | 17 | |
| α-helix | 102-118 | 17 | |
| α-helix | 123-125 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| BRCA1-A complex subunit RAP80 | A | protein | 63 | Homo sapiens | Q96RL1 (AlphaFold model) |
>2MKG_1 BRCA1-A complex subunit RAP80 (chains A) GPLGSRKIAQMTEEEQFALALKMSEQEAREVNSQEEEEEELLRKAIAESLNSCRPSDASA TRS
Molecular Basis for Impaired DNA Damage Response Function Associated with the RAP80 Delta E81 Defect. Anamika, Markin, C.J., Rout, M.K. et al. J Biol Chem (2014) 289:12852-12862. DOI 10.1074/jbc.M113.538280 · PubMed
Other PDB entries of the same protein (UniProt Q96RL1 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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