Spindlin 1 with crystallization epitope mutations H127D:L128D:T131R. Determined by X-ray diffraction at 1.87 Å resolution. Released 26 Nov 2025.
Explore 9T2Z in 3D Show helices and sheets RCSB PDB PDBe
9T2Z contains 8 α-helices and 18 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 |
|---|---|---|---|
| β-strand | 10-15 | 6 | 1 |
| β-strand | 23-32 | 10 | 1 |
| β-strand | 40-44 | 5 | 1 |
| β-strand | 49 | 1 | 2 |
| α-helix | 50 | 1 | |
| β-strand | 51-53 | 3 | 1 |
| β-strand | 61-66 | 6 | 1 |
| α-helix | 70-75 | 6 | |
| α-helix | 79-85 | 7 | |
| β-strand | 89-93 | 5 | 2 |
| β-strand | 103-111 | 9 | 2 |
| α-helix | 112 | 1 | |
| β-strand | 119-123 | 5 | 2 |
| β-strand | 128 | 1 | 3 |
| β-strand | 130-132 | 3 | 2 |
| α-helix | 134-139 | 6 | |
| β-strand | 143-145 | 3 | 2 |
| α-helix | 146-148 | 3 | |
| β-strand | 170-174 | 5 | 3 |
| α-helix | 179 | 1 | |
| β-strand | 180-188 | 9 | 3 |
| β-strand | 195-200 | 6 | 3 |
| β-strand | 205 | 1 | 1 |
| β-strand | 207-210 | 4 | 3 |
| α-helix | 214-216 | 3 | |
| β-strand | 220-221 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Spindlin-1 | A | protein | 222 | Homo sapiens | Q9Y657 (AlphaFold model) |
>9T2Z_1 Spindlin-1 (chains A) MPRRNIVGCRIQHGWKEGNGPVTQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELNKDER VSALEVLPDRVATSRISDADDADRMIGKAVEHMFETEDGSKDEWRGMVLARAPVMNTWFY ITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSK RTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTSAENLYFQ
A fast, parallel method for efficiently exploring crystallization behaviour of large numbers of protein variants. Fairhead, M., Strain-Damerell, C., Ye, M. et al. To be published.
Other PDB entries of the same protein (UniProt Q9Y657 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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