› 5tq2

X-ray diffraction
3.29Å resolution

Crystal structure of amino terminal domains of the NMDA receptor subunit GluN1 and GluN2A in complex with zinc at GluN1 and GluN2A

Released:
DOI: 10.2210/pdb5tq2/pdb
PDB entry 5tq2 coloured by chain, front view.
PDB entry 5tq2 coloured by chain, side view.
PDB entry 5tq2 coloured by chain, top view.
Source organisms:
Primary publication:
Molecular Basis for Subtype Specificity and High-Affinity Zinc Inhibition in the GluN1-GluN2A NMDA Receptor Amino-Terminal Domain.
Romero-Hernandez A, Simorowski N, Karakas E, Furukawa H
Neuron 92 1324-1336 (2016)
PMID: 27916457

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-230567 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Glutamate receptor ionotropic, NMDA 1 Chain: A
Molecule details ›
Chain: A
Length: 389 amino acids
Theoretical weight: 43.55 KDa
Source organism: Xenopus laevis
Expression system: Trichoplusia ni
UniProt: Gene name: grin1
Sequence domains: Receptor family ligand binding region
Structure domains: Rossmann fold
Glutamate receptor ionotropic, NMDA 2A Chain: B
Molecule details ›
Chain: B
Length: 360 amino acids
Theoretical weight: 40.57 KDa
Source organism: Rattus norvegicus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q00959 (Residues: 34-393; Coverage: 25%)
Gene name: Grin2a
Sequence domains: Receptor family ligand binding region
Structure domains: Rossmann fold
FAB, HEAVY CHAIN Chain: H
Molecule details ›
Chain: H
Length: 221 amino acids
Theoretical weight: 23.99 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
FAB, LIGHT CHAIN Chain: L
Molecule details ›
Chain: L
Length: 214 amino acids
Theoretical weight: 23.57 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins

Ligands and Environments

4 bound ligands:
Ligand ZN 2 x ZN
Ligand NAG 2 x NAG
Ligand SO4 4 x SO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P212121
Unit cell:
a: 78.163Å b: 117.826Å c: 158.992Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.224 0.261
Expression system: Trichoplusia ni

Quick links

Citations

17 review citations

Structure, function, and allosteric modulation of NMDA receptors.
Hansen et al. (2018)
16 more

2 mentions without citation

From bedside-to-bench: What disease-associated variants are teaching us about the NMDA receptor.
Amin et al. (2021)
1 more