K89 acetylated glucose-6-phosphate dehydrogenase (G6PD) in a complex with structural NADP+. Determined by X-ray diffraction at 2.46 Å resolution. Released 23 Aug 2023.
Explore 7ZVD in 3D Show helices and sheets RCSB PDB PDBe
7ZVD contains 33 α-helices and 20 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 | 32-37 | 6 | 1 |
| α-helix | 42-43 | 2 | |
| α-helix | 44-48 | 5 | |
| α-helix | 49-57 | 9 | |
| β-strand | 65-71 | 7 | 1 |
| α-helix | 77-84 | 8 | |
| α-helix | 96-101 | 6 | |
| α-helix | 102-103 | 2 | |
| β-strand | 105-109 | 5 | 1 |
| α-helix | 115-126 | 12 | |
| β-strand | 135-140 | 6 | 1 |
| α-helix | 144-146 | 3 | |
| α-helix | 147-157 | 11 | |
| β-strand | 165-170 | 6 | 1 |
| α-helix | 172 | 1 | |
| α-helix | 177-190 | 14 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-199 | 4 | 1 |
| α-helix | 201-204 | 4 | |
| α-helix | 206-216 | 11 | |
| β-strand | 230-238 | 9 | 2 |
| α-helix | 247-250 | 4 | |
| α-helix | 254-255 | 2 | |
| α-helix | 256-264 | 9 | |
| α-helix | 265-272 | 8 | |
| α-helix | 274-276 | 3 | |
| α-helix | 281-293 | 13 | |
| β-strand | 295 | 1 | 3 |
| α-helix | 296-299 | 4 | |
| α-helix | 300-302 | 3 | |
| β-strand | 303-309 | 7 | 2 |
| α-helix | 310 | 1 | |
| α-helix | 316-319 | 4 | |
| α-helix | 322-324 | 3 | |
| α-helix | 329 | 1 | |
| β-strand | 337-342 | 6 | 2 |
| β-strand | 344 | 1 | 3 |
| β-strand | 354-359 | 6 | 2 |
| β-strand | 362 | 1 | 4 |
| β-strand | 366-373 | 8 | 2 |
| α-helix | 374-376 | 3 | |
| β-strand | 389-395 | 7 | 2 |
| β-strand | 399-407 | 9 | 2 |
| β-strand | 415-423 | 9 | 2 |
| α-helix | 424-427 | 4 | |
| α-helix | 432-435 | 4 | |
| α-helix | 436-446 | 11 | |
| β-strand | 452-453 | 2 | 1 |
| α-helix | 455-475 | 21 | |
| α-helix | 477-479 | 3 | |
| β-strand | 480-483 | 4 | 2 |
| β-strand | 486 | 1 | 4 |
| α-helix | 490-498 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glucose-6-phosphate 1-dehydrogenase | N | protein | 484 | Homo sapiens | P11413 (AlphaFold model) |
>7ZVD_1 Glucose-6-phosphate 1-dehydrogenase (chains N) QSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPF FKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVY EAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEM VQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQM LCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDPT VPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQQCKR NELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCG SQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTY KWVN
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAP | NADP nicotinamide-adenine-dinucleotide phosphate | C21 H28 N7 O17 P3 | 1 |
Acetylation-dependent coupling between G6PD activity and apoptotic signaling. Wu, F., Muskat, N.H., Dvilansky, I. et al. Nat Commun (2023) 14:6208-6208. DOI 10.1038/s41467-023-41895-2 · 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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