Structure of the MAGEA4 MHD-RAD18 R6BD Complex. Determined by X-ray diffraction at 2.58 Å resolution. Released 5 Jun 2024.
Explore 9BD3 in 3D Show helices and sheets RCSB PDB PDBe
9BD3 contains 32 α-helices and 18 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 102-126 | 25 | |
| β-strand | 131-132 | 2 | 1 |
| α-helix | 133-139 | 7 | |
| α-helix | 142-147 | 6 | |
| α-helix | 148-158 | 11 | |
| α-helix | 159-163 | 5 | |
| β-strand | 165-171 | 7 | 1 |
| β-strand | 176-181 | 6 | 1 |
| α-helix | 182-184 | 3 | |
| β-strand | 191 | 1 | 2 |
| β-strand | 194 | 1 | 2 |
| α-helix | 200-213 | 14 | |
| β-strand | 217-218 | 2 | 3 |
| α-helix | 219-228 | 10 | |
| β-strand | 237 | 1 | 4 |
| β-strand | 241 | 1 | 4 |
| α-helix | 243-245 | 3 | |
| α-helix | 246-250 | 5 | |
| α-helix | 251-253 | 3 | |
| β-strand | 257-261 | 5 | 3 |
| α-helix | 262 | 1 | |
| β-strand | 270-274 | 5 | 3 |
| α-helix | 276-281 | 6 | |
| α-helix | 284-296 | 13 | |
| α-helix | 298-304 | 7 | |
| α-helix | 305-311 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 349-365 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 102-126 | 25 | |
| β-strand | 131-132 | 2 | 5 |
| α-helix | 133-139 | 7 | |
| α-helix | 142-147 | 6 | |
| α-helix | 148-163 | 16 | |
| β-strand | 165-171 | 7 | 5 |
| β-strand | 176-181 | 6 | 5 |
| α-helix | 182-184 | 3 | |
| α-helix | 200-213 | 14 | |
| β-strand | 217-218 | 2 | 6 |
| α-helix | 219-228 | 10 | |
| β-strand | 237 | 1 | 7 |
| β-strand | 241 | 1 | 7 |
| α-helix | 243-245 | 3 | |
| α-helix | 246-250 | 5 | |
| α-helix | 251-253 | 3 | |
| β-strand | 257-261 | 5 | 6 |
| β-strand | 270-274 | 5 | 6 |
| α-helix | 276-281 | 6 | |
| α-helix | 284-295 | 12 | |
| α-helix | 298-303 | 6 | |
| α-helix | 305-311 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 349-364 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Melanoma antigen A 4 | A, C | protein | 220 | Homo sapiens | P43358 (AlphaFold model) |
| E3 ubiquitin-protein ligase RAD18 | B, D | protein | 28 | Homo sapiens | Q9NS91 (AlphaFold model) |
>9BD3_1 Melanoma antigen A 4 (chains A, C) SNADAESLFREALSNKVDELAHFLLRKYRAKELVTKAEMLERVIKNYKRCFPVIFGKASE SLKMIFGIDVKEVDPTSNTYTLVTCLGLSYDGLLGNNQIFPKTGLLIIVLGTIAMEGDSA SEEEIWEELGVMGVYDGREHTVYGEPRKLLTQDWVQENYLEYRQVPGSNPARYEFLWGPR ALAETSYVKVLEHVVRVNARVRIAYPSLREAALLEEEEGV
>9BD3_2 E3 ubiquitin-protein ligase RAD18 (chains B, D) HSKYRKKHKSEFQLLVDQARKGYKKIAG
Crystal structure of MAGEA4 MHD-RAD18 R6BD reveals a flipped binding mode compared to AlphaFold2 prediction. Forker, K., Fleming, M.C., Pearce, K.H. et al. EMBO J (2024) 43:2835-2839. DOI 10.1038/s44318-024-00140-2 · PubMed
Other PDB entries of the same protein (UniProt P43358 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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