Crystal structure of human Glucose 6-phosphate Dehydrogenase mutant (A277C) complexed with G6P. Determined by X-ray diffraction at 2.65 Å resolution. Released 19 Apr 2017.
Explore 5UKW in 3D Show helices and sheets RCSB PDB PDBe
5UKW contains 30 α-helices and 18 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 | 85-88 | 4 | |
| α-helix | 92-94 | 3 | |
| α-helix | 95-103 | 9 | |
| 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 | 165-169 | 5 | 1 |
| α-helix | 177-190 | 14 | |
| α-helix | 193-195 | 3 | |
| β-strand | 196-198 | 3 | 1 |
| α-helix | 201-204 | 4 | |
| α-helix | 206-217 | 12 | |
| β-strand | 230-238 | 9 | 2 |
| α-helix | 247-251 | 5 | |
| α-helix | 255 | 1 | |
| 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 | 317-319 | 3 | |
| β-strand | 337-343 | 7 | 2 |
| β-strand | 344 | 1 | 3 |
| β-strand | 353-359 | 7 | 2 |
| β-strand | 366-373 | 8 | 2 |
| α-helix | 374-376 | 3 | |
| β-strand | 389-395 | 7 | 2 |
| β-strand | 399-407 | 9 | 2 |
| α-helix | 408 | 1 | |
| β-strand | 415-423 | 9 | 2 |
| α-helix | 433-435 | 3 | |
| α-helix | 436-446 | 11 | |
| β-strand | 453 | 1 | 1 |
| α-helix | 455-475 | 21 | |
| α-helix | 477-479 | 3 | |
| β-strand | 480-483 | 4 | 2 |
| α-helix | 490-498 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Glucose-6-phosphate 1-dehydrogenase | A | protein | 488 | Homo sapiens | P11413 (AlphaFold model) |
>5UKW_1 Glucose-6-phosphate 1-dehydrogenase (chains A) GGSEFSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQ SEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALP PTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYL GKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNH LLQMLCLVAMEKPCSTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYL DDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQ QCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILD VFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQY EGTYKWVN
| ID | Name | Formula | Copies |
|---|---|---|---|
| BG6 | 6-O-phosphono-beta-D-glucopyranose | C6 H13 O9 P | 1 |
Water and common crystallization additives (GOL) are not listed.
Mutations in the tetramer interface of human glucose-6-phosphate dehydrogenase reveals kinetic differences between oligomeric states. Ranzani, A.T., Cordeiro, A.T. FEBS Lett (2017) 591:1278-1284. DOI 10.1002/1873-3468.12638 · 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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