Crystal Structure of Human Mre11: Understanding Tumorigenic Mutations. Determined by X-ray diffraction at 3.0 Å resolution. Released 30 Nov 2011.
Explore 3T1I in 3D Show helices and sheets RCSB PDB PDBe
3T1I contains 60 α-helices and 96 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 | 9-11 | 3 | |
| β-strand | 12-18 | 7 | 1 |
| β-strand | 23 | 1 | 2 |
| α-helix | 35-49 | 15 | |
| β-strand | 54-57 | 4 | 1 |
| β-strand | 62 | 1 | 2 |
| α-helix | 69-83 | 15 | |
| β-strand | 84 | 1 | 3 |
| α-helix | 88-89 | 2 | |
| β-strand | 92-93 | 2 | 4 |
| β-strand | 118 | 1 | 3 |
| β-strand | 122-124 | 3 | 1 |
| β-strand | 133 | 1 | 5 |
| β-strand | 138 | 1 | 5 |
| α-helix | 140-147 | 8 | |
| β-strand | 150-152 | 3 | 1 |
| β-strand | 162-164 | 3 | 6 |
| β-strand | 167-171 | 5 | 4 |
| β-strand | 174-181 | 8 | 4 |
| α-helix | 186-194 | 9 | |
| β-strand | 198-200 | 3 | 6 |
| α-helix | 201-203 | 3 | |
| α-helix | 207-209 | 3 | |
| β-strand | 210-216 | 7 | 4 |
| α-helix | 231-233 | 3 | |
| β-strand | 240-243 | 4 | 4 |
| β-strand | 250-255 | 6 | 4 |
| β-strand | 262-265 | 4 | 4 |
| α-helix | 276-279 | 4 | |
| α-helix | 281-282 | 2 | |
| β-strand | 283-290 | 8 | 1 |
| β-strand | 293-300 | 8 | 1 |
| α-helix | 305-306 | 2 | |
| β-strand | 307-313 | 7 | 7 |
| α-helix | 314-316 | 3 | |
| α-helix | 328-350 | 23 | |
| β-strand | 362-368 | 7 | 7 |
| α-helix | 379-385 | 7 | |
| β-strand | 396-399 | 4 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Double-strand break repair protein MRE11A | A, B, C, D | protein | 431 | Homo sapiens | P49959 (AlphaFold model) |
>3T1I_1 Double-strand break repair protein MRE11A (chains A, B, C, D) MGSSHHHHHHSSGLVPRGSHMSTADALDDENTFKILVATDIHLGFMEKDAVRGNDTFVTL DEILRLAQENEVDFILLGGDLFHENKPSRKTLHTCLELLRKYCMGDRPVQFEILSDQSVN FGFSKFPWVNYQDGNLNISIPVFSIHGNHDDPTGADALCALDILSCAGFVNHFGRSMSVE KIDISPVLLQKGSTKIALYGLGSIPDERLYRMFVNKKVTMLRPKEDENSWFNLFVIHQNR SKHGSTNFIPEQFLDDFIDLVIWGHEHECKIAPTKNEQQLFYISQPGSSVVTSLSPGEAV KKHVGLLRIKGRKMNMHKIPLHTVRQFFMEDIVLANHPDIFNPDNPKVTQAIQSFCLEKI EEMLENAERERLGNSHQPEKPLVRLRVDYSGGFEPFSVLRFSQKFVDRVANPKDIIHFFR HREQKEKTGEE
Water and common crystallization additives (GOL) are not listed.
Crystal structure of human mre11: understanding tumorigenic mutations. Park, Y.B., Chae, J., Kim, Y. et al. Structure (2011) 19:1591-1602. DOI 10.1016/j.str.2011.09.010 · PubMed
Other PDB entries of the same protein (UniProt P49959 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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