The 2.6 Å refined structure of the escherichia coli recombinant saccharomyces cerevisiae flavocytochrome B2-sulphite complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 31 Aug 1994.
Explore 1LTD in 3D Show helices and sheets RCSB PDB PDBe
1LTD contains 55 α-helices and 36 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 | 13-18 | 6 | |
| β-strand | 26-28 | 3 | 1 |
| β-strand | 32-35 | 4 | 1 |
| α-helix | 40-42 | 3 | |
| α-helix | 47-52 | 6 | |
| β-strand | 57 | 1 | 1 |
| α-helix | 59-62 | 4 | |
| α-helix | 63-65 | 3 | |
| α-helix | 70-74 | 5 | |
| α-helix | 77-79 | 3 | |
| β-strand | 80-83 | 4 | 1 |
| α-helix | 90-92 | 3 | |
| β-strand | 93 | 1 | 1 |
| α-helix | 94-96 | 3 | |
| α-helix | 105-112 | 8 | |
| α-helix | 117-118 | 2 | |
| α-helix | 119-121 | 3 | |
| α-helix | 125-135 | 11 | |
| α-helix | 138-145 | 8 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-163 | 4 | |
| β-strand | 165-166 | 2 | 2 |
| β-strand | 178 | 1 | 3 |
| β-strand | 181-183 | 3 | 4 |
| β-strand | 186-188 | 3 | 4 |
| β-strand | 192-194 | 3 | 5 |
| α-helix | 200-202 | 3 | |
| α-helix | 210-217 | 8 | |
| β-strand | 225-228 | 4 | 5 |
| α-helix | 235-241 | 7 | |
| β-strand | 249-253 | 5 | 5 |
| α-helix | 259-272 | 14 | |
| β-strand | 277-280 | 4 | 5 |
| α-helix | 290-296 | 7 | |
| α-helix | 332-340 | 9 | |
| β-strand | 346-351 | 6 | 5 |
| α-helix | 354-362 | 9 | |
| β-strand | 367-370 | 4 | 5 |
| α-helix | 373-375 | 3 | |
| α-helix | 381-383 | 3 | |
| α-helix | 384-397 | 14 | |
| α-helix | 400-402 | 3 | |
| β-strand | 405-409 | 5 | 5 |
| α-helix | 415-424 | 10 | |
| β-strand | 428-431 | 4 | 5 |
| α-helix | 433-465 | 33 | |
| β-strand | 469 | 1 | 3 |
| α-helix | 470-472 | 3 | |
| α-helix | 475-477 | 3 | |
| β-strand | 478-479 | 2 | 2 |
| β-strand | 486-487 | 2 | 6 |
| α-helix | 489-491 | 3 | |
| α-helix | 494-499 | 6 | |
| α-helix | 505-508 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 104-115 | 12 | |
| α-helix | 117-118 | 2 | |
| α-helix | 119-121 | 3 | |
| α-helix | 125-135 | 11 | |
| α-helix | 138-145 | 8 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-163 | 4 | |
| β-strand | 165-166 | 2 | 7 |
| β-strand | 178 | 1 | 8 |
| β-strand | 181-182 | 2 | 9 |
| β-strand | 187-188 | 2 | 9 |
| β-strand | 192-194 | 3 | 10 |
| α-helix | 208-218 | 11 | |
| β-strand | 225-228 | 4 | 10 |
| α-helix | 235-241 | 7 | |
| β-strand | 250-253 | 4 | 10 |
| α-helix | 259-271 | 13 | |
| β-strand | 277-280 | 4 | 10 |
| α-helix | 290-295 | 6 | |
| α-helix | 332-340 | 9 | |
| β-strand | 346-351 | 6 | 10 |
| α-helix | 354-362 | 9 | |
| β-strand | 367-370 | 4 | 10 |
| β-strand | 381 | 1 | 2 |
| α-helix | 382-383 | 2 | |
| α-helix | 384-397 | 14 | |
| α-helix | 400-403 | 4 | |
| β-strand | 405-409 | 5 | 10 |
| α-helix | 415-424 | 10 | |
| β-strand | 429-431 | 3 | 10 |
| α-helix | 433-465 | 33 | |
| β-strand | 469 | 1 | 8 |
| α-helix | 475-477 | 3 | |
| β-strand | 478-479 | 2 | 7 |
| β-strand | 488-489 | 2 | 6 |
| α-helix | 490-492 | 3 | |
| α-helix | 494-499 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Flavocytochrome B2 | A, B | protein | 506 | Saccharomyces cerevisiae | P00175 (AlphaFold model) |
>1LTD_1 FLAVOCYTOCHROME B2 (chains A, B) MNKQKISPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFEPL HAPNVIDKYIAPEKKLGPLQGSMPPELVCPPYAPGETKEDIARKEQLKSLLPPLDNIINL YDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLG SHVDVPFYVSATALCKLGNPLEGEKDVARGCGQGVTKVPQMISTLASCSPEEIIEAAPSD KQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQREKDMKLKFSNTKAGPK AMKKTNVEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGV SGVVLSNHGGRQLDFSRAPIEVLAETMPILEQRNLKDKLEVFVDGGVRRGTDVLKALCLG AKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLLDLSTLKA RTVGVPNDVLYNEVYEGPTLTEFEDA
| ID | Name | Formula | Copies |
|---|---|---|---|
| SO3 | Sulfite ion | O3 S | 2 |
| FMN | Flavin mononucleotide | C17 H21 N4 O9 P | 2 |
| HEM | Protoporphyrin IX containing FE | C34 H32 Fe N4 O4 | 1 |
The 2.6-A refined structure of the Escherichia coli recombinant Saccharomyces cerevisiae flavocytochrome b2-sulfite complex. Tegoni, M., Cambillau, C. Protein Sci (1994) 3:303-313. PubMed
Other PDB entries of the same protein (UniProt P00175 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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