21wb

NZD domain of Mouse RAG1

Method: SOLUTION NMR Dmax: 75.0 Å Quality: GOOD

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

V(D)J recombination-activating protein 1

Mus musculus

UniProt P15919

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 89–223 Not recorded ZINC ION × 2 SOLUTION NMR mmCIF provides none of the parsed experimental conditions Resolution not provided

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.

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

View Construct and Data Evidence
UniProt name RAG1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–137; UniProt 89–223

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 21wb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 21wb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id21wb
Deposition date deposition_date2025-12-31
最后修订 last_revision2026-06-10
Structure title titleNZD domain of Mouse RAG1
Keywords keywordsZinc-binding protein, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier18.59
Radius of gyration Rg (electron density) rg_electron18.40
Forward intensity I(0) i0413175000.00
Molecular weight molecular_weight161500.0 kDa
Excluded volume excluded_volume198860 ų
Envelope volume envelope_volume64833 ų
Hydration-shell volume shell_volume24299 ų
Envelope diameter envelope_diameter79.3
Shell Rg shell_rg29.30
Envelope Rg envelope_rg23.21
Shape Rg shape_rg18.40
Total Rg total_rg18.82
Total atoms total_atoms22460
Residues n_residues1370
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 dmax75.0
Rg (real space) rg_real18.67
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real4.1320e+08
I(0) uncertainty (real space) i0_real_error5.7220e+06
Rg (reciprocal space) rg_reciprocal18.66
I(0) (reciprocal space) i0_reciprocal413200000.0000
Solution quality estimate total_estimate0.7618
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary73.0
Skewness Skewness skewness0.505
Kurtosis Kurtosis kurtosis0.095
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha889600.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.440; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.581; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)