5i57

Glutamate- and glycine-bound GluN1/GluN2A agonist binding domains

Method: X-RAY DIFFRACTION Dmax: 86.9 Å Quality: GOOD

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

Glutamate receptor ionotropic, NMDA 1,Glutamate receptor ionotropic, NMDA 1

Rattus norvegicus

UniProt P35439

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 415–565 Chain A; UniProt 684–821 Fragment:unp residues 415-565; 684-821 Glutamate receptor ionotropic, NMDA 2A,Glutamate receptor ionotropic, NMDA 2A × 1 (Q00959) GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.2 M ammonium sulfate and 16-22% PEG 4000 Resolution 1.70 Å R-free 0.222

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.

114 other PDB entries and 120 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDZ1_RAT
Isoform P35439-6
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–152; UniProt 415–565 Author chain A; PDBConstruct 155–292; UniProt 684–821

Glutamate receptor ionotropic, NMDA 2A,Glutamate receptor ionotropic, NMDA 2A

Rattus norvegicus

UniProt Q00959

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 402–539 Chain B; UniProt 661–800 Fragment:unp residues 402-539; 661-800 Glutamate receptor ionotropic, NMDA 1,Glutamate receptor ionotropic, NMDA 1 × 1 (P35439) GLY GLYCINE × 1 GLU GLUTAMIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.2 M ammonium sulfate and 16-22% PEG 4000 Resolution 1.70 Å R-free 0.222

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.

59 other PDB entries and 61 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–139; UniProt 402–539 Author chain B; PDBConstruct 142–281; UniProt 661–800

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 5i57

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5i57
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5i57
Deposition date deposition_date2016-02-14
Structure title titleGlutamate- and glycine-bound GluN1/GluN2A agonist binding domains
Keywords keywordsNMDA receptor, Antagonist, TRANSPORT PROTEIN, RECEPTOR; TRANSPORT PROTEIN, RECEPTOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.17
Radius of gyration Rg (electron density) rg_electron24.89
Forward intensity I(0) i065938400.00
Molecular weight molecular_weight63362.0 kDa
Excluded volume excluded_volume79435 ų
Envelope volume envelope_volume97184 ų
Hydration-shell volume shell_volume31932 ų
Envelope diameter envelope_diameter88.9
Shell Rg shell_rg32.61
Envelope Rg envelope_rg25.20
Shape Rg shape_rg24.86
Total Rg total_rg25.83
Total atoms total_atoms4451
Residues n_residues558
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 dmax86.9
Rg (real space) rg_real26.07
Rg uncertainty (real space) rg_real_error0.69
I(0) (real space) i0_real6.5940e+07
I(0) uncertainty (real space) i0_real_error1.0330e+06
Rg (reciprocal space) rg_reciprocal26.11
I(0) (reciprocal space) i0_reciprocal65940000.0000
Solution quality estimate total_estimate0.8803
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.4
Skewness Skewness skewness0.247
Kurtosis Kurtosis kurtosis-0.312
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14600000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.827; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5i57a_
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
Domain ID domain_idd5i57b_
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

CATH v4.4 (4 domains)

Domain ID domain_id5i57A01
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_id5i57A02
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_id5i57B01
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_id5i57B02
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)