Structure of CENP-E motor domain at 1.9 angstrom resolution. Determined by X-ray diffraction at 1.9 Å resolution. Released 10 Mar 2021.
Explore 6M4I in 3D Show helices and sheets RCSB PDB PDBe
6M4I contains 33 α-helices and 35 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 | 7-13 | 7 | 1 |
| α-helix | 14-16 | 3 | |
| β-strand | 31-34 | 4 | 2 |
| β-strand | 37-40 | 4 | 2 |
| β-strand | 46-48 | 3 | 2 |
| β-strand | 51-53 | 3 | 1 |
| α-helix | 59-62 | 4 | |
| α-helix | 63-67 | 5 | |
| α-helix | 68-75 | 8 | |
| β-strand | 80-85 | 6 | 1 |
| α-helix | 92-96 | 5 | |
| β-strand | 98-99 | 2 | 3 |
| β-strand | 102-103 | 2 | 3 |
| α-helix | 105-116 | 12 | |
| α-helix | 117-119 | 3 | |
| β-strand | 123-135 | 13 | 1 |
| β-strand | 138-141 | 4 | 1 |
| β-strand | 152 | 1 | 1 |
| β-strand | 154-156 | 3 | 4 |
| β-strand | 162-164 | 3 | 4 |
| β-strand | 170-172 | 3 | 1 |
| α-helix | 175-190 | 16 | |
| α-helix | 199-201 | 3 | |
| β-strand | 204-215 | 12 | 1 |
| β-strand | 226-235 | 10 | 1 |
| α-helix | 236-238 | 3 | |
| α-helix | 239-241 | 3 | |
| α-helix | 260-273 | 14 | |
| α-helix | 278-280 | 3 | |
| α-helix | 283-285 | 3 | |
| α-helix | 287-291 | 5 | |
| α-helix | 293-295 | 3 | |
| β-strand | 301-308 | 8 | 1 |
| α-helix | 314-326 | 13 | |
| β-strand | 337-338 | 2 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-13 | 7 | 5 |
| α-helix | 14-16 | 3 | |
| β-strand | 31-34 | 4 | 6 |
| β-strand | 37-40 | 4 | 6 |
| β-strand | 46-48 | 3 | 6 |
| β-strand | 51-53 | 3 | 5 |
| α-helix | 59-62 | 4 | |
| α-helix | 63-67 | 5 | |
| α-helix | 68-75 | 8 | |
| β-strand | 80-86 | 7 | 5 |
| α-helix | 92-96 | 5 | |
| β-strand | 98-99 | 2 | 7 |
| β-strand | 102-103 | 2 | 7 |
| α-helix | 105-116 | 12 | |
| α-helix | 117-119 | 3 | |
| β-strand | 123-135 | 13 | 5 |
| β-strand | 138-141 | 4 | 5 |
| β-strand | 154-156 | 3 | 8 |
| β-strand | 162-164 | 3 | 8 |
| β-strand | 170-172 | 3 | 5 |
| α-helix | 175-190 | 16 | |
| α-helix | 199-201 | 3 | |
| β-strand | 204-215 | 12 | 5 |
| β-strand | 226-235 | 10 | 5 |
| α-helix | 236-238 | 3 | |
| α-helix | 239-241 | 3 | |
| α-helix | 260-273 | 14 | |
| α-helix | 283-285 | 3 | |
| α-helix | 287-291 | 5 | |
| α-helix | 293-295 | 3 | |
| β-strand | 301-308 | 8 | 5 |
| α-helix | 314-326 | 13 | |
| β-strand | 337-338 | 2 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Centromere-associated protein E | A, B | protein | 353 | Homo sapiens | Q02224 (AlphaFold model) |
>6M4I_1 Centromere-associated protein E (chains A, B) MNHKVHMAEEGAVAVCVRVRPLNSREESLGETAQVYWKTDNNVIYQVDGSKSFNFDRVFH GNETTKNVYEEIAAPIIDSAIQGYNGTIFAYGQTASGKTYTMMGSEDHLGVIPRAIHDIF QKIKKFPDREFLLRVSYMEIYNETITDLLCGTQKMKPLIIREDVNRNVYVADLTEEVVYT SEMALKWITKGEKSRHYGETKMNQRSSRSHTIFRMILESREKGEPSNCEGSVKVSHLNLV DLAGSERAAQTGAAGVRLKEGCNINRSLFILGQVIKKLSDGQVGGFINYRDSKLTRILQN SLGGNPKTRIICTITPVSFDETLTALQFASTAKYMKNTPYVNEVSGSHHHHHH
Structure and comparison of the motor domain ofcentromere-associated protein E. Shibuya, A., Ogo, N., Sawada, J. et al. Acta Crystallogr D Biol Crystallogr (2021) 77:280-287. DOI 10.1107/S2059798321000176
Other PDB entries of the same protein (UniProt Q02224 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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