Crystal structure of eukaryotic Mre11 catalytic domain from Chaetomium thermophilum. Determined by X-ray diffraction at 2.78 Å resolution. Released 3 Jun 2015.
Explore 4YKE in 3D Show helices and sheets RCSB PDB PDBe
4YKE contains 33 α-helices and 50 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 | 9-15 | 7 | 1 |
| β-strand | 20 | 1 | 2 |
| α-helix | 32-46 | 15 | |
| β-strand | 51-54 | 4 | 1 |
| β-strand | 59 | 1 | 2 |
| α-helix | 66-80 | 15 | |
| β-strand | 81 | 1 | 3 |
| α-helix | 85-86 | 2 | |
| β-strand | 89-90 | 2 | 4 |
| α-helix | 94-97 | 4 | |
| α-helix | 106-108 | 3 | |
| β-strand | 112 | 1 | 5 |
| β-strand | 114 | 1 | 3 |
| β-strand | 118-120 | 3 | 1 |
| α-helix | 136-142 | 7 | |
| β-strand | 147-148 | 2 | 1 |
| β-strand | 158-160 | 3 | 6 |
| α-helix | 161-162 | 2 | |
| β-strand | 163-167 | 5 | 4 |
| β-strand | 170-176 | 7 | 4 |
| α-helix | 182-190 | 9 | |
| β-strand | 194-196 | 3 | 6 |
| α-helix | 206 | 1 | |
| β-strand | 207-212 | 6 | 4 |
| α-helix | 227-229 | 3 | |
| β-strand | 236-239 | 4 | 4 |
| β-strand | 246-251 | 6 | 4 |
| α-helix | 252 | 1 | |
| β-strand | 258-261 | 4 | 4 |
| α-helix | 272-275 | 4 | |
| α-helix | 277-278 | 2 | |
| β-strand | 279-286 | 8 | 1 |
| β-strand | 289-296 | 8 | 1 |
| α-helix | 301-302 | 2 | |
| β-strand | 303-309 | 7 | 7 |
| α-helix | 318-322 | 5 | |
| α-helix | 329-353 | 25 | |
| α-helix | 363-366 | 4 | |
| β-strand | 367-373 | 7 | 7 |
| α-helix | 387-392 | 6 | |
| β-strand | 395 | 1 | 8 |
| β-strand | 398 | 1 | 8 |
| β-strand | 405-408 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-15 | 7 | 9 |
| β-strand | 20 | 1 | 10 |
| α-helix | 32-46 | 15 | |
| β-strand | 51-54 | 4 | 9 |
| β-strand | 59 | 1 | 10 |
| α-helix | 66-80 | 15 | |
| β-strand | 81 | 1 | 11 |
| α-helix | 85-86 | 2 | |
| β-strand | 89-90 | 2 | 12 |
| α-helix | 106-108 | 3 | |
| β-strand | 112 | 1 | 5 |
| β-strand | 114 | 1 | 11 |
| β-strand | 118-120 | 3 | 9 |
| α-helix | 136-142 | 7 | |
| β-strand | 147-148 | 2 | 9 |
| β-strand | 158-160 | 3 | 13 |
| β-strand | 163-167 | 5 | 12 |
| β-strand | 170-177 | 8 | 12 |
| α-helix | 182-190 | 9 | |
| β-strand | 194-196 | 3 | 13 |
| α-helix | 206 | 1 | |
| β-strand | 207-212 | 6 | 12 |
| α-helix | 227-229 | 3 | |
| β-strand | 236-239 | 4 | 12 |
| β-strand | 246-251 | 6 | 12 |
| α-helix | 252 | 1 | |
| β-strand | 258-261 | 4 | 12 |
| α-helix | 272-275 | 4 | |
| α-helix | 277-278 | 2 | |
| β-strand | 279-286 | 8 | 9 |
| β-strand | 289-296 | 8 | 9 |
| α-helix | 301-302 | 2 | |
| β-strand | 303-309 | 7 | 14 |
| α-helix | 317-322 | 6 | |
| α-helix | 326-351 | 26 | |
| β-strand | 367-373 | 7 | 14 |
| α-helix | 387-392 | 6 | |
| β-strand | 395 | 1 | 15 |
| β-strand | 398 | 1 | 15 |
| β-strand | 405-408 | 4 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mre11 | A, B | protein | 548 | Chaetomium thermophilum | G0RYR3 (AlphaFold model) |
>4YKE_1 Mre11 (chains A, B) MPQTAGPDTIRILVSTDNHVGYEERDPIRKDDSWRTFDEIMQLARTKDVDMVLLGGDLFH DNKPSRKAMYQVMRSLRKNCLGMKPCELEFLSDPAEVFEGAFPHVNYYDPDINVSIPVFS IHGNHDDPSGDGHLCSLDLLQVAGLVNYFGRVPEADNIHVKPILLQKGKTKLALYGMSNV RDERIHRTFRDNKVRFYRPSQQTGDWFNLLTLHQNHYAHTPTGYLSENMLPDFLDLVIWG HEHECLIDPKKNPETGFHVMQPGSSIATSLVPGEAVPKHIAILSITGKSFEVEKIPLRTV RPFVIREITLATDKRFKGLEKKQDNRQEVTKRLMQIVEEMIAEANEMWRSLHEDSQDDED EEQPLPLIRLKVEYSSPEGTKFEVENPQRFSNRFAGKVANQNDVVHFYRKKTGTTRKPKE GKRELPEGIAEALEDSDSISVDALVQEFFAQQSLKILPQAPFGDAVNQFVSKDDKHAVEM FVMDSLSSQVRGLLQLDDDKINEGLDSHIEDFRKVMEKNFLSGQQKQAQRRRRFKEKAAA LEHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| MN | Manganese (II) ion | Mn | 4 |
Structure of the catalytic domain of Mre11 from Chaetomium thermophilum. Seifert, F.U., Lammens, K., Hopfner, K.P. Acta Crystallogr F Struct Biol Commun (2015) 71:752-757. DOI 10.1107/S2053230X15007566 · PubMed
Other PDB entries of the same protein (UniProt G0RYR3 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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