Crystal structure of the C-terminal calponin homology domain of alpha parvin. Determined by X-ray diffraction at 1.05 Å resolution. Released 28 Oct 2008.
Explore 2VZC in 3D Show helices and sheets RCSB PDB PDBe
2VZC contains 19 α-helices and 0 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 | 249-256 | 8 | |
| α-helix | 258-276 | 19 | |
| α-helix | 277-279 | 3 | |
| α-helix | 294-303 | 10 | |
| α-helix | 307-309 | 3 | |
| α-helix | 310-312 | 3 | |
| α-helix | 320-336 | 17 | |
| α-helix | 339-342 | 4 | |
| α-helix | 346-350 | 5 | |
| α-helix | 354-368 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 249-256 | 8 | |
| α-helix | 258-276 | 19 | |
| α-helix | 277-279 | 3 | |
| α-helix | 294-304 | 11 | |
| α-helix | 310-312 | 3 | |
| α-helix | 320-336 | 17 | |
| α-helix | 339-342 | 4 | |
| α-helix | 346-350 | 5 | |
| α-helix | 354-368 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-parvin | A, B | protein | 131 | HOMO SAPIENS | Q9NVD7 (AlphaFold model) |
>2VZC_1 ALPHA-PARVIN (chains A, B) SGRHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMG LLEGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVL YNLFTKYRNVE
| ID | Name | Formula | Copies |
|---|---|---|---|
| MRD | (4R)-2-methylpentane-2,4-diol | C6 H14 O2 | 1 |
Water and common crystallization additives (MPD, GOL, TRS) are not listed.
Structural Analysis of the Interactions between Paxillin Ld Motifs and Alpha-Parvin. Lorenz, S., Vakonakis, I., Lowe, E.D. et al. Structure (2008) 16:1521. DOI 10.1016/J.STR.2008.08.007 · PubMed
Other PDB entries of the same protein (UniProt Q9NVD7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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