7ujr

Cocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B

Method: X-RAY DIFFRACTION Dmax: 70.2 Å Quality: GOOD

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

Calcium/calmodulin-dependent protein kinase type II subunit alpha

Homo sapiens

UniProt Q9UQM7

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 7–274 Mutation:Q223K Glutamate receptor ionotropic, NMDA 2B × 1 (Q13224) EDO 1,2-ETHANEDIOL × 3 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 3350, 5% Ethanol Resolution 1.95 Å R-free 0.252

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.

21 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCC2A_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–268; UniProt 7–274

Glutamate receptor ionotropic, NMDA 2B

OrganismNot specified

UniProt Q13224

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 1289–1310 Not recorded Calcium/calmodulin-dependent protein kinase type II subunit alpha × 1 (Q9UQM7) EDO 1,2-ETHANEDIOL × 3 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.2;277 K;0.1M 1,3-bis(tris(hydroxymethyl)methylamino)propane, 0.1 M Ammonium sulfate, 20% PEG 3350, 5% Ethanol Resolution 1.95 Å R-free 0.252

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 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NMDE2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–22; UniProt 1289–1310

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 7ujr

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ujr
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7ujr
Deposition date deposition_date2022-03-31
Structure title titleCocrystal structure of human CaMKII-alpha (CAMK2A)kinase domain and GluN2B
Keywords keywordsCaMKII, Kinase, Human, CAMK2A, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.23
Radius of gyration Rg (electron density) rg_electron19.18
Forward intensity I(0) i017009100.00
Molecular weight molecular_weight31850.0 kDa
Excluded volume excluded_volume40140 ų
Envelope volume envelope_volume46395 ų
Hydration-shell volume shell_volume20311 ų
Envelope diameter envelope_diameter65.2
Shell Rg shell_rg25.50
Envelope Rg envelope_rg19.35
Shape Rg shape_rg19.19
Total Rg total_rg20.07
Total atoms total_atoms2251
Residues n_residues281
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 dmax70.2
Rg (real space) rg_real20.16
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real1.7010e+07
I(0) uncertainty (real space) i0_real_error2.0320e+05
Rg (reciprocal space) rg_reciprocal20.18
I(0) (reciprocal space) i0_reciprocal17010000.0000
Solution quality estimate total_estimate0.7870
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary25.1
Skewness Skewness skewness0.264
Kurtosis Kurtosis kurtosis-0.332
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4801000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.743; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)