Helix variant of the B1 domain from streptococcal protein G. Determined by X-ray diffraction at 2.0 Å resolution. Released 8 May 2002.
Explore 1EM7 in 3D Show helices and sheets RCSB PDB PDBe
1EM7 contains 1 α-helix and 4 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 | 2-8 | 7 | 1 |
| β-strand | 14-19 | 6 | 1 |
| α-helix | 23-36 | 14 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 51-55 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein G | A | protein | 56 | Streptococcus sp. | P06654 (AlphaFold model) |
>1EM7_1 PROTEIN G (chains A) TTYKLILNGKTLKGETTTEAVDAETAERVFKEYAKKNGVDGEWTYDDATKTFTVTE
Structure of a protein G helix variant suggests the importance of helix propensity and helix dipole interactions in protein design. Strop, P., Marinescu, A.M., Mayo, S.L. Protein Sci (2000) 9:1391-1394. PubMed
Other PDB entries of the same protein (UniProt P06654 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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