Crystal structure of the human MAGEA4. Determined by X-ray diffraction at 2.3 Å resolution. Released 10 Mar 2009.
Explore 2WA0 in 3D Show helices and sheets RCSB PDB PDBe
2WA0 contains 15 α-helices and 8 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 | 102-126 | 25 | |
| β-strand | 131-132 | 2 | 1 |
| α-helix | 133-139 | 7 | |
| α-helix | 145-147 | 3 | |
| α-helix | 148-158 | 11 | |
| α-helix | 159-163 | 5 | |
| β-strand | 165-169 | 5 | 1 |
| β-strand | 176-181 | 6 | 1 |
| α-helix | 182-184 | 3 | |
| α-helix | 200-213 | 14 | |
| β-strand | 217-218 | 2 | 2 |
| α-helix | 219-228 | 10 | |
| β-strand | 237 | 1 | 3 |
| β-strand | 241 | 1 | 3 |
| α-helix | 243-245 | 3 | |
| α-helix | 246-250 | 5 | |
| α-helix | 251-253 | 3 | |
| β-strand | 257-260 | 4 | 2 |
| β-strand | 271-274 | 4 | 2 |
| α-helix | 276-281 | 6 | |
| α-helix | 284-295 | 12 | |
| α-helix | 301-304 | 4 | |
| α-helix | 305-309 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Melanoma-associated antigen 4 | A | protein | 240 | HOMO SAPIENS | P43358 (AlphaFold model) |
>2WA0_1 MELANOMA-ASSOCIATED ANTIGEN 4 (chains A) MHHHHHHSSGVDLGTENLYFQSMDAESLFREALSNKVDELAHFLLRKYRAKELVTKAEML ERVIKNYKRCFPVIFGKASESLKMIFGIDVKEVDPTSNTYTLVTCLGLSYDGLLGNNQIF PKTGLLIIVLGTIAMEGDSASEEEIWEELGVMGVYDGREHTVYGEPRKLLTQDWVQENYL EYRQVPGSNPARYEFLWGPRALAETSYVKVLEHVVRVNARVRIAYPSLREAALLEEEEGV
Structures of Two Melanoma-Associated Antigens Suggest Allosteric Regulation of Effector Binding. Newman, J.A., Cooper, C.D.O., Roos, A.K. et al. PLoS One (2016) 11:48762. DOI 10.1371/JOURNAL.PONE.0148762 · 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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