5KDT: Human GluN1/GluN2A LBD

Structure of the human GluN1/GluN2A LBD in complex with GNE0723. Determined by X-ray diffraction at 2.44 Å resolution. Released 13 Jul 2016.

Method
X-ray diffraction
Resolution
2.44 Å
Organism
Homo sapiens
Chains
2
Atoms
4,607
Mol. weight
66.04 kDa
Ligands
GLU, 6RV, GLY
Released
13 Jul 2016

Explore 5KDT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5KDT contains 31 α-helices and 39 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: 15 helices, 18 β-strands

ElementResiduesLengthSheet
β-strand7-1261
β-strand1512
β-strand1912
β-strand20-2341
α-helix24-252
β-strand36-4381
β-strand51-5991
α-helix61-7212
β-strand76-8161
β-strand90-9123
β-strand94-9523
α-helix97-1037
β-strand109-11021
β-strand11514
α-helix118-1214
β-strand125-12621
β-strand131-140104
α-helix151-1544
α-helix156-1583
α-helix162-1632
β-strand165-16624
α-helix172-1809
α-helix182-1887
α-helix189-1913
α-helix196-2049
β-strand210-21454
α-helix215-2239
β-strand230-23234
α-helix233-2364
β-strand239-24464
β-strand247-24821
α-helix255-26814
α-helix270-2789
Chain B: 16 helices, 21 β-strands
ElementResiduesLengthSheet
α-helix61
β-strand7-1155
β-strand1416
β-strand1816
β-strand19-2245
α-helix23-242
α-helix29-313
β-strand3317
α-helix381
β-strand3917
α-helix40-412
β-strand43-4865
β-strand59-6575
α-helix67-7913
β-strand83-8755
β-strand96-9838
β-strand105-10738
α-helix109-1157
β-strand121-12225
β-strand12719
α-helix130-1334
β-strand136-13835
β-strand143-152109
α-helix163-1664
β-strand174-17529
β-strand177110
α-helix181-1888
α-helix190-1923
α-helix193-2008
β-strand204110
α-helix207-2159
β-strand221-22559
α-helix226-2338
β-strand239-251139
β-strand254-25635
α-helix262-27413
α-helix277-2859

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glutamate receptor ionotropic, NMDA 2AAprotein285Homo sapiensQ12879 (AlphaFold model)
Glutamate receptor ionotropic, NMDA 1Bprotein293Homo sapiensQ05586 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5KDT_1 Glutamate receptor ionotropic, NMDA 2A (chains A)
GSPDDNHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKG
FCIDILKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEER
SEVVDFSVPFVETGISVMVSRGTQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNN
YPYMHQYMTKFNQKGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFA
TTGYGIALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHN
Sequence of entity 2 (B), FASTA
>5KDT_2 Glutamate receptor ionotropic, NMDA 1 (chains B)
GSMSTRLKIVTIHQEPFVYVKPTLSDGTCKEEFTVNGDPVKKVICTGPNDTSPGSPRHTV
PQCCYGFCIDLLIKLARTMNFTYEVHLVADGKFGTQERVNNSNKKEWNGMMGELLSGQAD
MIVAPLTINNERAQYIEFSKPFKYQGLTILVKKGTRITGINDPRLRNPSDKFIYATVKQS
SVDIYFRRQVELSTMYRHMEKHNYESAAEAIQAVRDNKLHAFIWDSAVLEFEASQKCDLV
TTGELFFRSGFGIGMRKDSPWKQNVSLSILKSHENGFMEDLDKTWVRYQECDS

Ligands and cofactors

IDNameFormulaCopies
GLUGlutamic acidC5 H9 N O41
6RV(1~{R},2~{R})-2-[7-[[5-chloranyl-3-(trifluoromethyl)pyrazol-1-yl]methyl]-5-oxid…C16 H8 Cl F6 N5 O S1
GLYGlycineC2 H5 N O21

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

Primary citation

Discovery of GluN2A-Selective NMDA Receptor Positive Allosteric Modulators (PAMs): Tuning Deactivation Kinetics via Structure-Based Design. Volgraf, M., Sellers, B.D., Jiang, Y. et al. J Med Chem (2016) 59:2760-2779. DOI 10.1021/acs.jmedchem.5b02010 · PubMed

Other PDB entries of the same protein (UniProt Q12879 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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