Ferric soybean leghemoglobin complexed with nicotinate. Determined by X-ray diffraction at 2.3 Å resolution. Released 26 Jun 1996.
Explore 1FSL in 3D Show helices and sheets RCSB PDB PDBe
1FSL contains 18 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 | 5-20 | 16 | |
| α-helix | 22-36 | 15 | |
| α-helix | 40-43 | 4 | |
| α-helix | 45-47 | 3 | |
| α-helix | 57-79 | 23 | |
| α-helix | 86-91 | 6 | |
| α-helix | 99-117 | 19 | |
| α-helix | 118-120 | 3 | |
| α-helix | 123-141 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-19 | 15 | |
| α-helix | 22-36 | 15 | |
| α-helix | 40-43 | 4 | |
| α-helix | 45-47 | 3 | |
| α-helix | 56-78 | 23 | |
| α-helix | 86-91 | 6 | |
| α-helix | 99-117 | 19 | |
| α-helix | 118-120 | 3 | |
| α-helix | 123-140 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Leghemoglobin a | A, B | protein | 143 | Glycine max | P02238 (AlphaFold model) |
>1FSL_1 LEGHEMOGLOBIN A (chains A, B) VAFTEKQDALVSSSFEAFKANIPQYSVVFYTSILEKAPAAKDLFSFLANGVDPTNPKLTG HAEKLFALVRDSAGQLKASGTVVADAALGSVHAQKAVTDPQFVVVKEALLKTIKAAVGDK WSDELSRAWEVAYDELAAAIKKA
Structure of ferric soybean leghemoglobin a nicotinate at 2.3 A resolution. Ellis, P.J., Appleby, C.A., Guss, J.M. et al. Acta Crystallogr D Biol Crystallogr (1997) 53:302-310. DOI 10.1107/S0907444997000292 · PubMed
Other PDB entries of the same protein (UniProt P02238 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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