9T2Z: Spindlin-1

Spindlin 1 with crystallization epitope mutations H127D:L128D:T131R. Determined by X-ray diffraction at 1.87 Å resolution. Released 26 Nov 2025.

Method
X-ray diffraction
Resolution
1.87 Å
Organism
Homo sapiens
Chains
1
Atoms
1,828
Mol. weight
25.72 kDa
Released
26 Nov 2025

Explore 9T2Z in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 8 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand10-1561
β-strand23-32101
β-strand40-4451
β-strand4912
α-helix501
β-strand51-5331
β-strand61-6661
α-helix70-756
α-helix79-857
β-strand89-9352
β-strand103-11192
α-helix1121
β-strand119-12352
β-strand12813
β-strand130-13232
α-helix134-1396
β-strand143-14532
α-helix146-1483
β-strand170-17453
α-helix1791
β-strand180-18893
β-strand195-20063
β-strand20511
β-strand207-21043
α-helix214-2163
β-strand220-22123

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Spindlin-1Aprotein222Homo sapiensQ9Y657 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9T2Z_1 Spindlin-1 (chains A)
MPRRNIVGCRIQHGWKEGNGPVTQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELNKDER
VSALEVLPDRVATSRISDADDADRMIGKAVEHMFETEDGSKDEWRGMVLARAPVMNTWFY
ITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSK
RTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTSAENLYFQ

Primary citation

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:

Browse structure collections

About this viewer

MolViewer shows 9T2Z directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.