SH3 Domain of Human Lck. Determined by X-ray diffraction at 1.0 Å resolution. Released 7 Nov 2006.
Explore 2IIM in 3D Show helices and sheets RCSB PDB PDBe
2IIM contains 1 α-helix and 8 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 | 65-68 | 4 | 1 |
| β-strand | 72 | 1 | 2 |
| β-strand | 79 | 1 | 1 |
| β-strand | 82 | 1 | 2 |
| β-strand | 87-92 | 6 | 1 |
| β-strand | 97-102 | 6 | 1 |
| β-strand | 108-112 | 5 | 1 |
| α-helix | 113-115 | 3 | |
| β-strand | 116-118 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Proto-oncogene tyrosine-protein kinase LCK | A | protein | 62 | Homo sapiens | P06239 (AlphaFold model) |
>2IIM_1 Proto-oncogene tyrosine-protein kinase LCK (chains A) GSPLQDNLVIALHSYEPSHDGDLGFEKGEQLRILEQSGEWWKAQSLTTGQEGFIPFNFVA KA
Water and common crystallization additives (PG4) are not listed.
Crystal structure analysis and solution studies of human Lck-SH3; zinc-induced homodimerization competes with the binding of proline-rich motifs. Romir, J., Lilie, H., Egerer-Sieber, C. et al. J Mol Biol (2007) 365:1417-1428. DOI 10.1016/j.jmb.2006.10.058 · PubMed
Other PDB entries of the same protein (UniProt P06239 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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