3QEL: NMDA glutamate receptor subunit

Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2B in complex with ifenprodil. Determined by X-ray diffraction at 2.6 Å resolution. Released 15 Jun 2011.

Method
X-ray diffraction
Resolution
2.6 Å
Organisms
Xenopus laevis, Rattus norvegicus
Chains
4
Atoms
10,737
Mol. weight
171.68 kDa
Ligands
NAG, QEL
Released
15 Jun 2011

Explore 3QEL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3QEL contains 67 α-helices and 69 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.

Chain A: 20 helices, 17 β-strands

ElementResiduesLengthSheet
α-helix241
β-strand25-3391
α-helix36-5217
β-strand58-6691
α-helix67-682
α-helix71-777
α-helix78-825
α-helix83-853
β-strand87-9261
α-helix105-11410
β-strand118-12031
α-helix126-1294
β-strand137-13931
α-helix144-1463
α-helix147-15711
β-strand162-16872
α-helix171-18414
β-strand211-21882
α-helix226-2338
β-strand239-24352
α-helix246-25813
β-strand267-26932
α-helix273-2753
α-helix278-2814
α-helix283-2842
β-strand288-29252
α-helix298-31619
α-helix322-3265
α-helix339-3479
β-strand350-35453
β-strand357-36153
β-strand36611
β-strand367-36823
β-strand372-37872
β-strand381-38882
β-strand393-39532
α-helix399-4002
Chain B: 14 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand34-4294
α-helix47-504
β-strand65-7394
α-helix78-9114
β-strand94-10184
α-helix107-11913
β-strand123-12754
α-helix128-1314
β-strand143-14534
α-helix150-16314
β-strand168-17475
α-helix179-19113
β-strand198-20585
α-helix215-2206
β-strand227-23155
α-helix234-24512
β-strand255-25845
α-helix260-2634
α-helix2741
β-strand278-27925
β-strand28215
α-helix289-30820
α-helix327-3304
α-helix336-3394
β-strand343-34426
β-strand347-34826
β-strand35117
β-strand35717
β-strand362-36765
β-strand373-37975
β-strand384-38635
α-helix391-3922
Chain C: 18 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand25-3398
α-helix36-5217
β-strand58-6698
α-helix71-777
α-helix78-825
α-helix83-853
β-strand87-9268
α-helix105-11410
β-strand118-12038
α-helix126-1294
β-strand137-13938
α-helix144-1474
α-helix148-15710
β-strand162-16879
α-helix171-18313
β-strand211-21889
α-helix226-2349
β-strand239-24359
α-helix246-25813
β-strand267-27049
α-helix273-2753
α-helix278-2825
α-helix283-2842
β-strand288-29259
α-helix298-31619
α-helix324-3263
α-helix339-3479
β-strand351-354410
β-strand357-359310
β-strand360-361211
β-strand36618
β-strand367-368211
β-strand372-37879
β-strand381-38889
β-strand393-39539
α-helix399-4002
Chain D: 15 helices, 16 β-strands
ElementResiduesLengthSheet
β-strand34-42912
α-helix47-504
β-strand65-73912
α-helix78-8912
β-strand94-100712
α-helix107-11913
β-strand123-127512
α-helix128-1314
β-strand143-145312
α-helix150-16314
β-strand168-174713
α-helix179-19214
β-strand198-205813
α-helix215-2206
β-strand227-231513
α-helix234-24613
β-strand255-258413
α-helix260-2634
α-helix2741
β-strand278-282513
α-helix289-30012
α-helix304-3118
α-helix315-3173
α-helix336-3394
β-strand351114
β-strand356112
β-strand357114
β-strand362-367613
β-strand373-378613
β-strand385-386213
α-helix391-3933

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
NMDA glutamate receptor subunitA, Cprotein383Xenopus laevisA0A1L8F5J9 (AlphaFold model)
Glutamate [NMDA] receptor subunit epsilon-2B, Dprotein364Rattus norvegicusQ00960 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>3QEL_1 NMDA glutamate receptor subunit (chains A, C)
DPKIVNIGAVLSTKKHEQIFREAVNQANKRHFTRKIQLQATSVTHRPNAIQMALSVCEDL
ISSQVYAILVSHPPAPTDHLTPTPISYTAGFYRIPVIGLTTRMSIYSDKSIHLSFLRTVP
PYSHQALVWFEMMRLFNWNHVILIVSDDHEGRAAQKKLETLLEGKESKSKKRNYENLDQL
SYDNKRGPKADKVLQFEPGTKNLTALLLEAKELEARVIILSASEDDATAVYKSAAMLDMT
GAGYVWLVGEREISGSALRYAPDGIIGLQLINGKNESAHISDAVAVVAQAIHELFEMENI
TDPPRGCVGNTNIWKTGPLFKRVLMSSKYPDGVTGRIEFNEDGDRKFAQYSIMNLQNRKL
VQVGIFNGSYIIQNDRKIIWPGG
Sequence of entity 2 (B, D), FASTA
>3QEL_2 Glutamate [NMDA] receptor subunit epsilon-2 (chains B, D)
SPPSIGIAVILVGTSDEVAIKDAHEKDDFHHLSVVPRVELVAMNETDPKSIITRICDLMS
DRKIQGVVFADDTDQEAIAQILDFISAQTLTPILGIHGGSSMIMADKDESSMFFQFGPSI
EQQASVMLNIMEEYDWYIFSIVTTYFPGYQDFVNKIRSTIENSFVGWELEEVLLLDMSLD
DGDSKIQNQLKKLQSPIILLYCTKEEATYIFEVANSVGLTGYGYTWIVPSLVAGDTDTVP
SEFPTGLISVSYDEWDYGLPARVRDGIAIITTAASDMLSEHSFIPEPKSSCYNTHEKRIY
QSNMLNRYLINVTFEGRDLSFSEDGYQMHPKLVIILLNKERKWERVGKWKDKSLQMKYYV
WPRM

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O66
QEL4-[(1R,2S)-2-(4-benzylpiperidin-1-yl)-1-hydroxypropyl]phenolC21 H27 N O22

Water and common crystallization additives (NA) are not listed.

Primary citation

Subunit arrangement and phenylethanolamine binding in GluN1/GluN2B NMDA receptors. Karakas, E., Simorowski, N., Furukawa, H. Nature (2011) 475:249-253. DOI 10.1038/nature10180 · PubMed

Other PDB entries of the same protein (UniProt A0A1L8F5J9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 3QEL directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.