4JWX: GluN2A ligand-binding core

GluN2A ligand-binding core in complex with propyl-NHP5G. Determined by X-ray diffraction at 1.5 Å resolution. Released 29 May 2013.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Rattus norvegicus
Chains: 1
Atoms: 2,844
Mol. weight: 31.62 kDa
Ligands: 1N4
Released: 29 May 2013

Explore 4JWX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4JWX contains 17 α-helices and 19 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.

Chain A: 17 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	8	1
β-strand	9-13	5	1
β-strand	16	1	2
β-strand	20	1	2
β-strand	21-24	4	1
α-helix	25-26	2
β-strand	37-44	8	1
β-strand	52-60	9	1
α-helix	62-74	13
β-strand	78-82	5	1
β-strand	91-92	2	3
β-strand	95-96	2	3
α-helix	98-104	7
β-strand	110-111	2	1
β-strand	116	1	4
α-helix	119-122	4
β-strand	125-127	3	1
α-helix	128-130	3
β-strand	132-134	3	4
β-strand	136-141	6	5
α-helix	152-155	4
α-helix	157-159	3
α-helix	163-164	2
β-strand	166-167	2	5
α-helix	173-181	9
α-helix	183-189	7
α-helix	190-192	3
α-helix	197-205	9
β-strand	211-215	5	5
α-helix	216-224	9
β-strand	231-235	5	5
α-helix	239-241	3
β-strand	243-245	3	4
β-strand	248-250	3	1
α-helix	256-269	14
α-helix	271-279	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GluN2A	A	protein	280	Rattus norvegicus	Q00959 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4JWX_1 GluN2A (chains A)
NHLSIVTLEEAPFVIVEDIDPLTETCVRNTVPCRKFVKINNSTNEGMNVKKCCKGFCIDI
LKKLSRTVKFTYDLYLVTNGKHGKKVNNVWNGMIGEVVYQRAVMAVGSLTINEERSEVVD
FSVPFVETGISVMVSRGTQVTGLSDKKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPYMH
QYMTRFNQRGVEDALVSLKTGKLDAFIYDAAVLNYKAGRDEGCKLVTIGSGYIFATTGYG
IALQKGSPWKRQIDLALLQFVGDGEMEELETLWLTGICHA

Ligands and cofactors

ID	Name	Formula	Copies
1N4	(2R)-amino(1-hydroxy-4-propyl-1H-pyrazol-5-yl)ethanoic acid	C8 H13 N3 O3	1

Primary citation

Structural determinants of agonist efficacy at the glutamate binding site of N-methyl-d-aspartate receptors. Hansen, K.B., Tajima, N., Risgaard, R. et al. Mol Pharmacol (2013) 84:114-127. DOI 10.1124/mol.113.085803 · PubMed

Other PDB entries of the same protein (UniProt Q00959 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5U8C 1.6 Å, Crystal structure of GLUN1/GLUN2A ligand-binding domain in complex with glycine and…
9GJ1 1.62 Å, NMDA bound to compound 339
6UZ6 1.66 Å, Crystal structure of GLUN1/GLUN2A-4M mutant ligand-binding domain in complex with…
2A5S 1.7 Å, Crystal Structure Of The NR2A Ligand Binding Core In Complex With Glutamate
5I57 1.7 Å, Glutamate- and glycine-bound GluN1/GluN2A agonist binding domains
9NYZ 1.71 Å, Crystal structure of DCKA/glutamate-bound GluN1/GluN2A agonist binding domains with…
4NF8 1.86 Å, Crystal structure of GluN1/GluN2A ligand-binding domain in complex with glycine and…
6UZR 1.87 Å, Crystal structure of GLUN1/GLUN2A ligand-binding domain in complex with glycine and…
4NF5 1.9 Å, Crystal structure of GluN1/GluN2A ligand-binding domain in complex with glycine and D-AP5
6UZG 1.94 Å, Crystal structure of GLUN1/GLUN2A-4M mutant ligand-binding domain in complex with…
9GIB 1.95 Å, NMDA bound to compound 380
5VII 1.95 Å, Crystal structure of GluN1/GluN2A NMDA receptor agonist binding domains with glycine and…

Browse structure collections

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