1rmd

RAG1 DIMERIZATION DOMAIN

Method: X-RAY DIFFRACTION Dmax: 65.1 Å Quality: GOOD

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

RAG1

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 265–380 Fragment:ZINC-BINDING DIMERIZATION DOMAIN ZN ZINC ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.5;5-10 % PEG 4K, 100MM HEPES, PH 7.5, 10% ETHYLENE GLYCOL Resolution 2.10 Å R-free 0.257

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 1–116; UniProt 265–380

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 1rmd

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1rmd
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1rmd
Deposition date deposition_date1997-01-10
Structure title titleRAG1 DIMERIZATION DOMAIN
Keywords keywords;RAG1, V(D)J RECOMBINATION, ANTIBODY, MAD, RING FINGER, ZINC BINUCLEAR CLUSTER, ZINC FINGER, DNA-BINDING PROTEIN, DNA BINDING PROTEIN ;; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.80
Radius of gyration Rg (electron density) rg_electron15.91
Forward intensity I(0) i03871110.00
Molecular weight molecular_weight13378.0 kDa
Excluded volume excluded_volume16506 ų
Envelope volume envelope_volume20092 ų
Hydration-shell volume shell_volume11418 ų
Envelope diameter envelope_diameter61.8
Shell Rg shell_rg20.76
Envelope Rg envelope_rg16.56
Shape Rg shape_rg15.96
Total Rg total_rg16.77
Total atoms total_atoms915
Residues n_residues116
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 dmax65.1
Rg (real space) rg_real16.88
Rg uncertainty (real space) rg_real_error0.68
I(0) (real space) i0_real3.8710e+06
I(0) uncertainty (real space) i0_real_error5.3090e+04
Rg (reciprocal space) rg_reciprocal16.87
I(0) (reciprocal space) i0_reciprocal3871000.0000
Solution quality estimate total_estimate0.7865
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.8
Skewness Skewness skewness0.475
Kurtosis Kurtosis kurtosis-0.100
Angular range angular_range— – 0.4750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha372100.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.512; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.685; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1rmda1
Class classg — Small proteins
Fold Fold foldg.37 — beta-beta-alpha zinc fingers
Superfamily Superfamily superfamilyg.37.1 — beta-beta-alpha zinc fingers
Family Family familyg.37.1.1 — Classic zinc finger, C2H2
Domain ID domain_idd1rmda2
Class classg — Small proteins
Fold Fold foldg.44 — RING/U-box
Superfamily Superfamily superfamilyg.44.1 — RING/U-box
Family Family familyg.44.1.1 — RING finger domain, C3HC4

CATH v4.4 (2 domains)

Domain ID domain_id1rmdA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology40 — Herpes Virus-1
Homologous superfamily homologous superfamily10 — Zinc/RING finger domain, C3HC4 (zinc finger)
Domain ID domain_id1rmdA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily60 — Classic Zinc Finger

8. Citations (1)

9. Files and Curves (10)