1my7

NF-kappaB p65 subunit dimerization domain homodimer N202R mutation

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

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

NF-kappaB p65 (RelA) subunit

Mus musculus

UniProt Q04207

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 191–304 Chain B; UniProt 191–304 Fragment:residues 191 - 304 (dimerization domain) Mutation:N202R No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.l M sodium HEPES, 0.2 M sodium tartrate, 2 M ammonium sulfate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 1.49 Å R-free 0.247

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.

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TF65_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–114; UniProt 191–304 Author chain B; PDBConstruct 1–114; UniProt 191–304

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 1my7

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1my7
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1my7
Deposition date deposition_date2002-10-03
Structure title titleNF-kappaB p65 subunit dimerization domain homodimer N202R mutation
Keywords keywords;Immunoglobulin, Ig, beta-sandwich, beta-sheet, homodimerDNA-binding, Transcription regulation, Activator, Nuclear protein, Phosphorylation, TRANSCRIPTION ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.19
Radius of gyration Rg (electron density) rg_electron19.11
Forward intensity I(0) i010911300.00
Molecular weight molecular_weight23806.0 kDa
Excluded volume excluded_volume29452 ų
Envelope volume envelope_volume35941 ų
Hydration-shell volume shell_volume16221 ų
Envelope diameter envelope_diameter67.1
Shell Rg shell_rg24.60
Envelope Rg envelope_rg19.45
Shape Rg shape_rg19.12
Total Rg total_rg19.89
Total atoms total_atoms1673
Residues n_residues209
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_real20.17
Rg uncertainty (real space) rg_real_error0.45
I(0) (real space) i0_real1.0910e+07
I(0) uncertainty (real space) i0_real_error1.4130e+05
Rg (reciprocal space) rg_reciprocal20.17
I(0) (reciprocal space) i0_reciprocal10910000.0000
Solution quality estimate total_estimate0.8222
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.3
Skewness Skewness skewness0.269
Kurtosis Kurtosis kurtosis-0.487
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2785000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1my7a_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.1 — NF-kappa-B/REL/DORSAL transcription factors, C-terminal domain
Domain ID domain_idd1my7b_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.1 — NF-kappa-B/REL/DORSAL transcription factors, C-terminal domain

CATH v4.4 (2 domains)

Domain ID domain_id1my7A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1my7B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins

8. Citations (1)

9. Files and Curves (10)