Crystal Structure of the N-terminal region of AlphaII-spectrin Tetramerization Domain. Determined by X-ray diffraction at 2.3 Å resolution. Released 13 Oct 2009.
Explore 3F31 in 3D Show helices and sheets RCSB PDB PDBe
3F31 contains 11 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 | 14-25 | 12 | |
| α-helix | 30-66 | 37 | |
| α-helix | 78-94 | 17 | |
| α-helix | 97-112 | 16 | |
| α-helix | 117-146 | 30 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-11 | 3 | |
| α-helix | 12-32 | 21 | |
| α-helix | 34-66 | 33 | |
| α-helix | 78-94 | 17 | |
| α-helix | 97-111 | 15 | |
| α-helix | 117-143 | 27 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Spectrin alpha chain, brain | A, B | protein | 149 | Homo sapiens | Q13813 (AlphaFold model) |
>3F31_1 Spectrin alpha chain, brain (chains A, B) GSMDPSGVKVLETAEDIQERRQQVLDRYHRFKELSTLRRQKLEDSYRFQFFQRDAEELEK WIQEKLQIASDENYKDPTNLQGKLQKHQAFEAEVQANSGAIVKLDETGNLMISEGHFASE TIRTRLMELHRQWELLLEKMREKGIKLLQ
Crystal structure of the nonerythroid alpha-spectrin tetramerization site reveals differences between erythroid and nonerythroid spectrin tetramer formation. Mehboob, S., Song, Y., Witek, M. et al. J Biol Chem (2010) 285:14572-14584. DOI 10.1074/jbc.M109.080028 · PubMed
Other PDB entries of the same protein (UniProt Q13813 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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