1oy3

CRYSTAL STRUCTURE OF AN IKBBETA/NF-KB P65 HOMODIMER COMPLEX

Method: X-RAY DIFFRACTION Dmax: 91.9 Å Quality: GOOD

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

Transcription factor p65

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 heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 191–326 Chain C; UniProt 191–326 Fragment:p65 dimerization domain transcription factor inhibitor I-kappa-B-beta × 1 (Q60778) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.8;291 K;PEG 8000, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.05 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 B; PDBConstruct 1–136; UniProt 191–326 Author chain C; PDBConstruct 1–136; UniProt 191–326

transcription factor inhibitor I-kappa-B-beta

Mus musculus

UniProt Q60778

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 50–331 Not recorded Transcription factor p65 × 2 (Q04207) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.8;291 K;PEG 8000, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.05 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IKBB_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–282; UniProt 50–331

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 1oy3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1oy3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1oy3
Deposition date deposition_date2003-04-03
Structure title titleCRYSTAL STRUCTURE OF AN IKBBETA/NF-KB P65 HOMODIMER COMPLEX
Keywords keywordsProtein-protein complex, Transcription factors, Nuclear localization, 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_guinier25.24
Radius of gyration Rg (electron density) rg_electron24.47
Forward intensity I(0) i046935400.00
Molecular weight molecular_weight51657.0 kDa
Excluded volume excluded_volume64087 ų
Envelope volume envelope_volume79937 ų
Hydration-shell volume shell_volume27177 ų
Envelope diameter envelope_diameter93.8
Shell Rg shell_rg31.52
Envelope Rg envelope_rg24.79
Shape Rg shape_rg24.48
Total Rg total_rg25.23
Total atoms total_atoms3640
Residues n_residues467
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 dmax91.9
Rg (real space) rg_real25.20
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real4.6940e+07
I(0) uncertainty (real space) i0_real_error7.5520e+05
Rg (reciprocal space) rg_reciprocal25.22
I(0) (reciprocal space) i0_reciprocal46940000.0000
Solution quality estimate total_estimate0.8412
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.345
Kurtosis Kurtosis kurtosis-0.165
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13480000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.677; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.909; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd1oy3b_
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_idd1oy3c_
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_idd1oy3d_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamilyd.211.1 — Ankyrin repeat
Family Family familyd.211.1.1 — Ankyrin repeat

CATH v4.4 (3 domains)

Domain ID domain_id1oy3B00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1oy3C00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id1oy3D00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily20 — Ankyrin repeat-containing domain

8. Citations (1)

9. Files and Curves (10)