Crystal structure of glucose-6-phosphate dehydrogenase W509A mutant in complex with catalytic NADP+. Determined by X-ray diffraction at 3.1 Å resolution. Released 27 Jan 2021.
Explore 6VA0 in 3D Show helices and sheets RCSB PDB PDBe
6VA0 contains 26 α-helices and 16 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 | 31-37 | 7 | 1 |
| α-helix | 42-43 | 2 | |
| α-helix | 44-48 | 5 | |
| α-helix | 49-57 | 9 | |
| β-strand | 64-71 | 8 | 1 |
| α-helix | 77-84 | 8 | |
| α-helix | 85-87 | 3 | |
| α-helix | 92-94 | 3 | |
| α-helix | 95-103 | 9 | |
| β-strand | 105-109 | 5 | 1 |
| α-helix | 115-127 | 13 | |
| β-strand | 135-140 | 6 | 1 |
| α-helix | 144-146 | 3 | |
| α-helix | 147-157 | 11 | |
| β-strand | 165-169 | 5 | 1 |
| α-helix | 177-188 | 12 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 1 |
| α-helix | 207-221 | 15 | |
| β-strand | 230-238 | 9 | 2 |
| α-helix | 247-250 | 4 | |
| α-helix | 255 | 1 | |
| α-helix | 256-264 | 9 | |
| α-helix | 265-272 | 8 | |
| α-helix | 273-276 | 4 | |
| α-helix | 281-292 | 12 | |
| β-strand | 295 | 1 | 3 |
| α-helix | 300-302 | 3 | |
| β-strand | 303-309 | 7 | 2 |
| α-helix | 316-318 | 3 | |
| α-helix | 329 | 1 | |
| β-strand | 337-343 | 7 | 2 |
| β-strand | 344 | 1 | 3 |
| β-strand | 353-359 | 7 | 2 |
| β-strand | 367-373 | 7 | 2 |
| β-strand | 389-393 | 5 | 2 |
| α-helix | 436-446 | 11 | |
| β-strand | 453 | 1 | 1 |
| α-helix | 455-475 | 21 | |
| α-helix | 479 | 1 | |
| β-strand | 480-483 | 4 | 2 |
| α-helix | 490-498 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glucose-6-phosphate 1-dehydrogenase | A | protein | 515 | Homo sapiens | P11413 (AlphaFold model) |
>6VA0_1 Glucose-6-phosphate 1-dehydrogenase (chains A) MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGL LPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQR LNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSS DRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEP FGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQA NNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGK ALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESEL DLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPI PYIYGSRGPTEADELMKRVGFQYEGTYKAVNPHKL
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAP | NADP nicotinamide-adenine-dinucleotide phosphate | C21 H28 N7 O17 P3 | 1 |
Long-range structural defects by pathogenic mutations in most severe glucose-6-phosphate dehydrogenase deficiency. Horikoshi, N., Hwang, S., Gati, C. et al. Proc Natl Acad Sci U S A (2021) 118. DOI 10.1073/pnas.2022790118 · 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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