7SNI: G6PD-D200N tetramer

Structure of G6PD-D200N tetramer bound to NADP+ and G6P. Determined by electron microscopy at 2.5 Å resolution. Released 13 Jul 2022.

Method
Electron microscopy
Resolution
2.5 Å
Organism
Homo sapiens
Chains
4
Atoms
16,533
Mol. weight
248.6 kDa
Ligands
NAP, BG6
Released
13 Jul 2022

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

Secondary structure: helices and β-sheets

7SNI contains 126 α-helices and 72 β-strands across 4 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.

Chains A and B: 31 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix29-313
β-strand32-3761
α-helix42-432
α-helix44-485
α-helix49-579
β-strand65-7171
α-helix77-8812
α-helix92-943
α-helix95-1039
β-strand105-10951
α-helix115-12713
α-helix1341
β-strand135-14061
α-helix144-1463
α-helix147-15711
β-strand165-16951
α-helix177-18812
β-strand196-19831
α-helix201-2044
α-helix206-21611
β-strand230-23892
α-helix247-2559
α-helix256-2649
α-helix265-2728
α-helix273-2764
α-helix281-29212
β-strand29513
α-helix296-2994
α-helix300-3023
β-strand303-30972
α-helix316-3194
α-helix322-3243
α-helix3291
β-strand337-34372
β-strand34413
β-strand353-35972
β-strand366-37382
α-helix374-3763
β-strand389-39572
β-strand399-40792
α-helix4081
β-strand415-42392
α-helix433-4353
α-helix436-44611
β-strand45311
α-helix455-47521
α-helix477-4793
β-strand480-48342
α-helix490-49910
Chains C and D: 32 helices, 18 β-strands
ElementResiduesLengthSheet
α-helix29-313
β-strand32-3766
α-helix42-432
α-helix44-485
α-helix49-579
β-strand65-7176
α-helix77-8812
α-helix92-943
α-helix95-1039
β-strand105-10956
α-helix115-12713
α-helix1341
β-strand135-14066
α-helix144-1463
α-helix147-15711
β-strand165-16956
α-helix177-19014
β-strand196-19836
α-helix201-2044
α-helix206-21611
β-strand230-23897
α-helix247-2515
α-helix254-2552
α-helix256-2649
α-helix265-2728
α-helix273-2764
α-helix281-29212
β-strand29518
α-helix296-2994
α-helix300-3023
β-strand303-30977
α-helix316-3194
α-helix322-3243
α-helix3291
β-strand337-34377
β-strand34418
β-strand353-35977
β-strand366-37387
α-helix374-3763
β-strand389-39577
β-strand399-40797
α-helix4081
β-strand415-42397
α-helix433-4353
α-helix436-44611
β-strand45316
α-helix455-47521
α-helix477-4793
β-strand480-48347
α-helix490-49910

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glucose-6-phosphate 1-dehydrogenaseA, B, C, Dprotein523Homo sapiensP11413 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>7SNI_1 Glucose-6-phosphate 1-dehydrogenase (chains A, B, C, D)
MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGL
LPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQR
LNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSS
DRLSNHISSLFREDQIYRINHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEP
FGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQA
NNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGK
ALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESEL
DLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPI
PYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKLLEHHHHHH

Ligands and cofactors

IDNameFormulaCopies
NAPNADP nicotinamide-adenine-dinucleotide phosphateC21 H28 N7 O17 P38
BG66-O-phosphono-beta-D-glucopyranoseC6 H13 O9 P4

Primary citation

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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