Structure of G6PD-WT dimer. Determined by electron microscopy at 3.5 Å resolution. Released 13 Jul 2022.
Explore 7SNF in 3D Show helices and sheets RCSB PDB PDBe
7SNF contains 57 α-helices and 44 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 |
|---|---|---|---|
| β-strand | 32-37 | 6 | 1 |
| α-helix | 42-43 | 2 | |
| α-helix | 44-48 | 5 | |
| α-helix | 49-57 | 9 | |
| β-strand | 65-70 | 6 | 1 |
| β-strand | 71 | 1 | 2 |
| α-helix | 77-88 | 12 | |
| α-helix | 92-94 | 3 | |
| α-helix | 95-101 | 7 | |
| β-strand | 105-106 | 2 | 1 |
| β-strand | 109 | 1 | 2 |
| α-helix | 115-126 | 12 | |
| β-strand | 135-136 | 2 | 1 |
| β-strand | 138-140 | 3 | 1 |
| α-helix | 144-146 | 3 | |
| α-helix | 147-157 | 11 | |
| β-strand | 167-169 | 3 | 1 |
| α-helix | 170 | 1 | |
| α-helix | 172 | 1 | |
| α-helix | 177-190 | 14 | |
| β-strand | 196-198 | 3 | 1 |
| α-helix | 208-216 | 9 | |
| β-strand | 230-238 | 9 | 3 |
| α-helix | 255 | 1 | |
| α-helix | 256-264 | 9 | |
| α-helix | 265-272 | 8 | |
| α-helix | 281-293 | 13 | |
| α-helix | 300-302 | 3 | |
| β-strand | 303-309 | 7 | 3 |
| α-helix | 329 | 1 | |
| β-strand | 337-343 | 7 | 3 |
| β-strand | 344 | 1 | 4 |
| β-strand | 350 | 1 | 4 |
| β-strand | 353-356 | 4 | 3 |
| β-strand | 366-373 | 8 | 3 |
| α-helix | 374-376 | 3 | |
| β-strand | 391-393 | 3 | 5 |
| β-strand | 399-402 | 4 | 5 |
| β-strand | 405-407 | 3 | 6 |
| α-helix | 408 | 1 | |
| β-strand | 415-417 | 3 | 6 |
| β-strand | 420-421 | 2 | 5 |
| α-helix | 436-446 | 11 | |
| α-helix | 455-464 | 10 | |
| α-helix | 466-475 | 10 | |
| α-helix | 479 | 1 | |
| β-strand | 480-483 | 4 | 3 |
| α-helix | 490-499 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 32-37 | 6 | 7 |
| α-helix | 42-43 | 2 | |
| α-helix | 44-48 | 5 | |
| α-helix | 49-57 | 9 | |
| β-strand | 65-67 | 3 | 7 |
| β-strand | 70 | 1 | 7 |
| β-strand | 71 | 1 | 8 |
| α-helix | 77-84 | 8 | |
| α-helix | 86-88 | 3 | |
| α-helix | 92-94 | 3 | |
| α-helix | 95-103 | 9 | |
| β-strand | 109 | 1 | 8 |
| α-helix | 115-126 | 12 | |
| β-strand | 135-140 | 6 | 7 |
| α-helix | 144-146 | 3 | |
| α-helix | 147-157 | 11 | |
| β-strand | 167-169 | 3 | 7 |
| α-helix | 170 | 1 | |
| α-helix | 172 | 1 | |
| α-helix | 177-190 | 14 | |
| α-helix | 193-195 | 3 | |
| β-strand | 197-198 | 2 | 7 |
| α-helix | 207-216 | 10 | |
| β-strand | 230-235 | 6 | 9 |
| β-strand | 238 | 1 | 10 |
| α-helix | 247-250 | 4 | |
| α-helix | 255 | 1 | |
| α-helix | 256-264 | 9 | |
| α-helix | 265-272 | 8 | |
| α-helix | 281-293 | 13 | |
| α-helix | 300-302 | 3 | |
| β-strand | 304-309 | 6 | 11 |
| α-helix | 317-319 | 3 | |
| α-helix | 329 | 1 | |
| β-strand | 337-339 | 3 | 11 |
| β-strand | 342 | 1 | 9 |
| α-helix | 347-349 | 3 | |
| β-strand | 354-356 | 3 | 9 |
| β-strand | 366 | 1 | 10 |
| β-strand | 369-373 | 5 | 9 |
| α-helix | 374-376 | 3 | |
| α-helix | 386-388 | 3 | |
| β-strand | 391-393 | 3 | 12 |
| β-strand | 399-402 | 4 | 12 |
| β-strand | 405-407 | 3 | 13 |
| α-helix | 408 | 1 | |
| β-strand | 415-417 | 3 | 13 |
| β-strand | 420-421 | 2 | 12 |
| α-helix | 436-446 | 11 | |
| α-helix | 455-475 | 21 | |
| α-helix | 479 | 1 | |
| β-strand | 480-483 | 4 | 11 |
| α-helix | 490-499 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glucose-6-phosphate 1-dehydrogenase | A, B | protein | 523 | Homo sapiens | P11413 (AlphaFold model) |
>7SNF_1 Glucose-6-phosphate 1-dehydrogenase (chains A, B) MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGL LPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQR LNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSS DRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEP FGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQA NNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGK ALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESEL DLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPI PYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKLLEHHHHHH
Allosteric role of a structural NADP + molecule in glucose-6-phosphate dehydrogenase activity. Wei, X., Kixmoeller, K., Baltrusaitis, E. et al. Proc Natl Acad Sci U S A (2022) 119:e2119695119-e2119695119. DOI 10.1073/pnas.2119695119 · PubMed
Other PDB entries of the same protein (UniProt P11413 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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