2jwo

A PHD finger motif in the C-terminus of RAG2 modulates recombination activity

Method: SOLUTION NMR Dmax: 59.1 Å Quality: REASONABLE

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

V(D)J recombination-activating protein 2

Mus musculus

UniProt P21784

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 414–487 Fragment:PHD finger motif: Residues 414-487 ZN ZINC ION × 2 SOLUTION NMR NMR measurement conditions:pH 7.2;298 K;Ionic strength (raw mmCIF value) 0;Pressure ambient NMR sample composition:0.5 mM [U-99% 13C; U-99% 15N] RAG2 PHD domain, 90% H2O/10% D2O | 90% H2O/10% D2O 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.

33 other PDB entries and 43 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAG2_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 9–82; UniProt 414–487

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 2jwo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2jwo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2jwo
Deposition date deposition_date2007-10-17
Structure title titleA PHD finger motif in the C-terminus of RAG2 modulates recombination activity
Keywords keywords;V(D)J recombination, phosphoinositide signaling, RAG2, PHD domain, DNA recombination, DNA-binding, Endonuclease, Hydrolase, Nuclease, Nucleus, RECOMBINATION ;; RECOMBINATION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier13.54
Radius of gyration Rg (electron density) rg_electron13.56
Forward intensity I(0) i0570895000.00
Molecular weight molecular_weight189520.0 kDa
Excluded volume excluded_volume230830 ų
Envelope volume envelope_volume36350 ų
Hydration-shell volume shell_volume16909 ų
Envelope diameter envelope_diameter65.0
Shell Rg shell_rg24.35
Envelope Rg envelope_rg19.07
Shape Rg shape_rg13.60
Total Rg total_rg13.70
Total atoms total_atoms25060
Residues n_residues1640
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 dmax59.1
Rg (real space) rg_real13.57
Rg uncertainty (real space) rg_real_error0.66
I(0) (real space) i0_real5.7090e+08
I(0) uncertainty (real space) i0_real_error7.1440e+06
Rg (reciprocal space) rg_reciprocal13.57
I(0) (reciprocal space) i0_reciprocal570900000.0000
Solution quality estimate total_estimate0.7164
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary16.4
Skewness Skewness skewness0.443
Kurtosis Kurtosis kurtosis0.221
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha162600.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.307; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.386; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd2jwoa1
Class classg — Small proteins
Fold Fold foldg.50 — FYVE/PHD zinc finger
Superfamily Superfamily superfamilyg.50.1 — FYVE/PHD zinc finger
Family Family familyg.50.1.2 — PHD domain
Domain ID domain_idd2jwoa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id2jwoA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology160 — Double Stranded RNA Binding Domain
Homologous superfamily homologous superfamily290 — Rag2 PHD finger

8. Citations (1)

9. Files and Curves (10)