Structure of the WW domain of PIN1 in complex with a human phosphorylated Smad3 derived peptide. Determined by solution NMR. Released 6 Jul 2011.
Explore 2LB3 in 3D Show helices and sheets RCSB PDB PDBe
2LB3 contains 0 α-helices and 3 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 | 17-20 | 4 | 1 |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 35-37 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | A | protein | 36 | Homo sapiens | Q13526 (AlphaFold model) |
| Mothers against decapentaplegic homolog 2 | B | protein | 8 | Homo sapiens | Q15796 (AlphaFold model) |
>2LB3_1 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (chains A) KLPPGWEKRMSRSSGRVYYFNHITNASQWERPSGNS
>2LB3_2 Mothers against decapentaplegic homolog 2 (chains B) IPETPPPG
A Smad action turnover switch operated by WW domain readers of a phosphoserine code. Aragon, E., Goerner, N., Zaromytidou, A.I. et al. Genes Dev (2011) 25:1275-1288. DOI 10.1101/gad.2060811 · PubMed
Other PDB entries of the same protein (UniProt Q13526 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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