5tpa

Structure of the human GluN1/GluN2A LBD in complex with compound 9 (GNE3500)

Method: X-RAY DIFFRACTION Dmax: 86.2 Å Quality: GOOD

1. Protein Identity and Related Structures Protein Identity & Related Structures

Glutamate receptor ionotropic, NMDA 2A

Homo sapiens

UniProt Q12879

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 401–539 Chain A; UniProt 661–802 Fragment:Ligand binding domain (UNP residues 401-539, GT linker, UNP residues 661-802) Glutamate receptor ionotropic, NMDA 1 × 1 (Q05586) GLU GLUTAMIC ACID × 1 7H2 (1R,2R)-2-(2-{[5-chloro-3-(trifluoromethyl)-1H-pyrazol-1-yl]methyl}-7-methyl-4-oxo-4H-pyrido[1,2-a]pyrimidin-6-yl)cyclopropane-1-carbonitrile × 1 GLY GLYCINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;0.1 M HEPES, pH 7.0, 10-13% PEG8000, 2 mM calcium acetate Resolution 2.48 Å R-free 0.241

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

35 other PDB entries and 40 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE1_HUMAN
Isoform Q12879-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–141; UniProt 401–539 Author chain A; PDBConstruct 144–285; UniProt 661–802

Glutamate receptor ionotropic, NMDA 1

Homo sapiens

UniProt Q05586

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 415–565 Chain B; UniProt 684–821 Fragment:UNP residues 394-544, GT linker, UNP residues 663-800 Glutamate receptor ionotropic, NMDA 2A × 1 (Q12879) GLU GLUTAMIC ACID × 1 7H2 (1R,2R)-2-(2-{[5-chloro-3-(trifluoromethyl)-1H-pyrazol-1-yl]methyl}-7-methyl-4-oxo-4H-pyrido[1,2-a]pyrimidin-6-yl)cyclopropane-1-carbonitrile × 1 GLY GLYCINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;277 K;0.1 M HEPES, pH 7.0, 10-13% PEG8000, 2 mM calcium acetate Resolution 2.48 Å R-free 0.241

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

83 other PDB entries and 86 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDZ1_HUMAN
Isoform Q05586-5
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–153; UniProt 415–565 Author chain B; PDBConstruct 156–293; UniProt 684–821

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 5tpa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5tpa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5tpa
Deposition date deposition_date2016-10-20
Structure title titleStructure of the human GluN1/GluN2A LBD in complex with compound 9 (GNE3500)
Keywords keywordsNMDA receptor, glutamate, glycine, calcium channel, membrane, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier25.96
Radius of gyration Rg (electron density) rg_electron24.77
Forward intensity I(0) i062747900.00
Molecular weight molecular_weight62298.0 kDa
Excluded volume excluded_volume78188 ų
Envelope volume envelope_volume95003 ų
Hydration-shell volume shell_volume31366 ų
Envelope diameter envelope_diameter89.0
Shell Rg shell_rg32.69
Envelope Rg envelope_rg25.13
Shape Rg shape_rg24.75
Total Rg total_rg25.72
Total atoms total_atoms4376
Residues n_residues554
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax86.2
Rg (real space) rg_real25.88
Rg uncertainty (real space) rg_real_error0.57
I(0) (real space) i0_real6.2750e+07
I(0) uncertainty (real space) i0_real_error8.8850e+05
Rg (reciprocal space) rg_reciprocal25.91
I(0) (reciprocal space) i0_reciprocal62750000.0000
Solution quality estimate total_estimate0.8867
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.1
Skewness Skewness skewness0.263
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13430000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5tpaa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.0 — automated matches
Domain ID domain_idd5tpab_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.94 — Periplasmic binding protein-like II
Superfamily Superfamily superfamilyc.94.1 — Periplasmic binding protein-like II
Family Family familyc.94.1.1 — Phosphate binding protein-like

CATH v4.4 (4 domains)

Domain ID domain_id5tpaA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5tpaA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5tpaB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II
Domain ID domain_id5tpaB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology190 — D-Maltodextrin-Binding Protein; domain 2
Homologous superfamily homologous superfamily10 — Periplasmic binding protein-like II

8. Citations (1)

9. Files and Curves (10)