7SEH: Glucose-6-phosphate 1-dehydrogenase

Glucose-6-phosphate 1-dehydrogenase (K403QdLtL). Determined by X-ray diffraction at 2.9 Å resolution. Released 17 Aug 2022.

Method
X-ray diffraction
Resolution
2.9 Å
Organism
Homo sapiens
Chains
2
Atoms
7,291
Mol. weight
121.25 kDa
Ligands
NAP
Released
17 Aug 2022

Explore 7SEH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7SEH contains 55 α-helices and 33 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.

Chain A: 30 helices, 16 β-strands

ElementResiduesLengthSheet
β-strand31-3771
α-helix42-432
α-helix44-485
α-helix49-579
β-strand64-7181
α-helix77-848
α-helix92-943
α-helix95-10410
β-strand105-10951
α-helix115-12612
α-helix131-1333
β-strand135-14061
α-helix147-1537
α-helix154-1585
β-strand165-16951
α-helix1701
α-helix1721
α-helix177-18711
α-helix193-1953
β-strand196-19831
α-helix207-22115
α-helix222-2243
β-strand230-23892
α-helix247-2504
α-helix2551
α-helix256-2649
α-helix265-2728
α-helix281-29313
β-strand29513
α-helix296-2994
α-helix300-3023
β-strand303-30972
α-helix3101
α-helix3291
β-strand337-34372
β-strand34413
β-strand353-35972
β-strand366-37382
α-helix374-3752
β-strand388-39362
β-strand401-40442
α-helix436-44611
α-helix455-47521
α-helix4791
β-strand480-48342
α-helix490-4989
Chain B: 25 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand32-3764
α-helix421
α-helix43-486
α-helix49-579
β-strand65-7174
α-helix77-826
α-helix86-883
α-helix95-1028
β-strand105-10954
α-helix115-12713
β-strand135-14064
α-helix147-1537
α-helix154-1585
β-strand165-16954
α-helix177-19014
α-helix193-1953
β-strand196-19834
α-helix207-22115
α-helix222-2243
β-strand230-23895
α-helix247-2504
α-helix254-2552
α-helix256-2649
α-helix265-2728
α-helix281-29313
β-strand29516
α-helix300-3023
β-strand303-30975
α-helix316-3194
β-strand337-34265
β-strand34416
β-strand354-35965
β-strand366-37385
α-helix385-3873
β-strand388-39255
β-strand401-40445
α-helix437-4459
β-strand45314
α-helix455-47420
α-helix477-4793
β-strand480-48345
α-helix491-4988

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glucose-6-phosphate 1-dehydrogenaseA, Bprotein520Homo sapiensP11413 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>7SEH_1 Glucose-6-phosphate 1-dehydrogenase (chains A, B)
GSHMMAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLF
RDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAA
SYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRD
LQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILT
FKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPCSTNSDDVRDEKVKVLKCIS
EVQANNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFIL
RCGKALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTQMMTKKPGMFFNPE
ESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEK
PKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKLC

Ligands and cofactors

IDNameFormulaCopies
NAPNADP nicotinamide-adenine-dinucleotide phosphateC21 H28 N7 O17 P32

Primary citation

Stabilization of glucose-6-phosphate dehydrogenase oligomers enhances catalytic activity and stability of clinical variants. Garcia, A.A., Mathews, I.I., Horikoshi, N. et al. J Biol Chem (2022) 298:101610-101610. DOI 10.1016/j.jbc.2022.101610 · PubMed

Other PDB entries of the same protein (UniProt P11413 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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