Crystal structure of alpha-parvin CH1 dimer. Determined by X-ray diffraction at 2.35 Å resolution. Released 22 Apr 2026.
Explore 9UIU in 3D Show helices and sheets RCSB PDB PDBe
9UIU contains 18 α-helices and 4 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 |
|---|---|---|---|
| α-helix | 92-108 | 17 | |
| α-helix | 119-122 | 4 | |
| α-helix | 127-141 | 15 | |
| α-helix | 148-149 | 2 | |
| α-helix | 150-168 | 19 | |
| α-helix | 172-174 | 3 | |
| α-helix | 179-183 | 5 | |
| α-helix | 187-200 | 14 | |
| α-helix | 207-208 | 2 | |
| β-strand | 212-221 | 10 | 1 |
| β-strand | 224-233 | 10 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 92-108 | 17 | |
| α-helix | 110-112 | 3 | |
| α-helix | 119-122 | 4 | |
| α-helix | 127-141 | 15 | |
| α-helix | 150-168 | 19 | |
| α-helix | 172-174 | 3 | |
| α-helix | 179-183 | 5 | |
| α-helix | 187-200 | 14 | |
| α-helix | 207-208 | 2 | |
| β-strand | 212-221 | 10 | 1 |
| β-strand | 224-233 | 10 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-parvin | A, B | protein | 160 | Homo sapiens | Q9NVD7 (AlphaFold model) |
>9UIU_1 Alpha-parvin (chains A, B) GPGSEFSDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLESEKLNV AEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKSLVAILHLLVALSQYFRA PIRLPDHVSIQVVVVQKREGILQSRQIQEEITGNTEALSG
Alpha-Parvin as a novel mechanosensor crucial for adhesion tensional homeostasis. Guo, K., Pei, L., Zhang, T. et al. To be published.
Other PDB entries of the same protein (UniProt Q9NVD7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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