1sb0

Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb

Method: SOLUTION NMR Dmax: 96.6 Å Quality: GOOD

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

protein CBP

Mus musculus

UniProt P45481

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 580–666 Fragment:KIX domain protein c-Myb × 1 (P06876) SOLUTION NMR NMR measurement conditions:pH 5.5;27 K;Ionic strength (raw mmCIF value) 50 mM;Pressure ambient NMR sample composition:20 mM Tris d11 acetate d4; 50 mM NaCl; 2 mM NaN3; pH 5.5 | 90% H20; 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.

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

View Construct and Data Evidence
UniProt name CBP_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–87; UniProt 580–666

protein c-Myb

Mus musculus

UniProt P06876

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 291–315 Fragment:transcriptional activation domain protein CBP × 1 (P45481) SOLUTION NMR NMR measurement conditions:pH 5.5;27 K;Ionic strength (raw mmCIF value) 50 mM;Pressure ambient NMR sample composition:20 mM Tris d11 acetate d4; 50 mM NaCl; 2 mM NaN3; pH 5.5 | 90% H20; 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.

18 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYB_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–25; UniProt 291–315

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 1sb0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1sb0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1sb0
Deposition date deposition_date2004-02-09
Structure title titleSolution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb
Keywords keywordsCREB-binding protein; transcriptional activation; constitutive activation; LXXLL motif; Myb; KIX, Transcription; TRANSCRIPTION
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier25.92
Radius of gyration Rg (electron density) rg_electron25.47
Forward intensity I(0) i01028670000.00
Molecular weight molecular_weight265550.0 kDa
Excluded volume excluded_volume333250 ų
Envelope volume envelope_volume199420 ų
Hydration-shell volume shell_volume51871 ų
Envelope diameter envelope_diameter104.8
Shell Rg shell_rg39.58
Envelope Rg envelope_rg30.40
Shape Rg shape_rg25.40
Total Rg total_rg26.36
Total atoms total_atoms37880
Residues n_residues2240
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 dmax96.6
Rg (real space) rg_real25.89
Rg uncertainty (real space) rg_real_error0.89
I(0) (real space) i0_real1.0290e+09
I(0) uncertainty (real space) i0_real_error1.5530e+07
Rg (reciprocal space) rg_reciprocal25.90
I(0) (reciprocal space) i0_reciprocal1029000000.0000
Solution quality estimate total_estimate0.8309
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.1
Skewness Skewness skewness0.360
Kurtosis Kurtosis kurtosis-0.226
Angular range angular_range— – 0.3050 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha28170000.0000
Real-space data points n_real_points62
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.626; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.920; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1sb0a_
Class classa — All alpha proteins
Fold Fold folda.12 — Kix domain of CBP (creb binding protein)
Superfamily Superfamily superfamilya.12.1 — Kix domain of CBP (creb binding protein)
Family Family familya.12.1.1 — Kix domain of CBP (creb binding protein)

CATH v4.4 (1 domains)

Domain ID domain_id1sb0A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily20 — Coactivator CBP, KIX domain

8. Citations (1)

9. Files and Curves (10)