Protein Z in complex with an in vitro selected affibody. Determined by X-ray diffraction at 2.3 Å resolution. Released 18 Mar 2003.
Explore 1LP1 in 3D Show helices and sheets RCSB PDB PDBe
1LP1 contains 7 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 | 5-17 | 13 | |
| α-helix | 24-36 | 13 | |
| α-helix | 38-40 | 3 | |
| α-helix | 41-54 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-16 | 11 | |
| α-helix | 24-36 | 13 | |
| α-helix | 41-54 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Affibody binding protein Z | A | protein | 58 | Staphylococcus aureus | |
| Immunoglobulin G binding protein A | B | protein | 58 | Staphylococcus aureus | P38507 (AlphaFold model) |
>1LP1_1 Affibody binding protein Z (chains A) VDNKFNKELSVAGREIVTLPNLNDPQKKAFIFSLWDDPSQSANLLAEAKKLNDAQAPK
>1LP1_2 Immunoglobulin G binding protein A (chains B) VDNKFNKEQQNAFYEILHLPNLNEEQRNAFIQSLKDDPSQSANLLAEAKKLNDAQAPK
| ID | Name | Formula | Copies |
|---|---|---|---|
| MG | Magnesium ion | Mg | 1 |
Water and common crystallization additives (SO4) are not listed.
Structural basis for recognition by an in vitro evolved affibody. Hogbom, M., Eklund, M., Nygren, P.A. et al. Proc Natl Acad Sci U S A (2003) 100:3191-3196. DOI 10.1073/pnas.0436100100 · PubMed
Other PDB entries of the same protein (UniProt P38507 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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