Crystal structure of CENP-M solved by native-SAD phasing. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Dec 2014.
Explore 4WAU in 3D Show helices and sheets RCSB PDB PDBe
4WAU contains 15 α-helices and 10 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 16-21 | 6 | 1 |
| α-helix | 25-36 | 12 | |
| α-helix | 43 | 1 | |
| β-strand | 44-49 | 6 | 1 |
| β-strand | 65-71 | 7 | 1 |
| α-helix | 75-84 | 10 | |
| α-helix | 85-87 | 3 | |
| α-helix | 90-93 | 4 | |
| β-strand | 97-102 | 6 | 1 |
| α-helix | 111-123 | 13 | |
| β-strand | 128-130 | 3 | 1 |
| α-helix | 136-153 | 18 | |
| α-helix | 165-168 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 16-21 | 6 | 2 |
| α-helix | 25-37 | 13 | |
| β-strand | 44-49 | 6 | 2 |
| β-strand | 65-71 | 7 | 2 |
| α-helix | 75-84 | 10 | |
| α-helix | 85-87 | 3 | |
| α-helix | 90-93 | 4 | |
| β-strand | 97-102 | 6 | 2 |
| α-helix | 111-123 | 13 | |
| β-strand | 128-130 | 3 | 2 |
| α-helix | 136-153 | 18 | |
| α-helix | 162-168 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Centromere protein M | A, B | protein | 176 | Homo sapiens | Q9NSP4 (AlphaFold model) |
>4WAU_1 Centromere protein M (chains A, B) GPLGSMSVLRPLDKLPGLNTATILLVGTEDALLQQLADSMLKEDCASELKVHLAKSLPLP SSVNRPRIDLIVFVVNLHSKYSLQNTEESLRHVDASFFLGKVCFLATGAGRESHCSIHRH TVVKLAHTYQSPLLYCDLEVEGFRATMAQRLVRVLQICAGHVPGVSALNLLSLLRS
Fast native-SAD phasing for routine macromolecular structure determination. Weinert, T., Olieric, V., Waltersperger, S. et al. Nat Methods (2015) 12:131-133. DOI 10.1038/nmeth.3211 · PubMed
Other PDB entries of the same protein (UniProt Q9NSP4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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