The NMR structure of alpha-parvin CH2/paxillin LD1 complex. Determined by solution NMR. Released 27 May 2008.
Explore 2K2R in 3D Show helices and sheets RCSB PDB PDBe
2K2R contains 8 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 | 6-13 | 8 | |
| α-helix | 15-36 | 22 | |
| α-helix | 43-46 | 4 | |
| α-helix | 51-61 | 11 | |
| α-helix | 77-94 | 18 | |
| α-helix | 103-107 | 5 | |
| α-helix | 112-125 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-9 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-parvin | A | protein | 129 | Homo sapiens | Q9NVD7 (AlphaFold model) |
| Paxillin | B | protein | 10 | P49023 (AlphaFold model) |
>2K2R_1 Alpha-parvin (chains A) RHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLL EGYFVPLHSFFLTPDSFEQKVLNVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYN LFTKYRNVE
>2K2R_2 Paxillin (chains B) DLDALLADLE
The Structure of {alpha}-Parvin CH2-Paxillin LD1 Complex Reveals a Novel Modular Recognition for Focal Adhesion Assembly. Wang, X., Fukuda, K., Byeon, I.J. et al. J Biol Chem (2008) 283:21113-21119. DOI 10.1074/jbc.M801270200 · 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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