1io4

CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN-CBFBETA CORE DOMAIN HETERODIMER AND C/EBPBETA BZIP HOMODIMER BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER

Method: X-RAY DIFFRACTION Dmax: 99.9 Å Quality: EXCELLENT

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

CAAT/ENHANCER BINDING PROTEIN BETA

Homo sapiens

UniProt P17676

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 259–336 Chain B; UniProt 259–336 Fragment:BZIP DOMAIN CSF-1R PROMOTER × 1 CSF-1R PROMOTER × 1 RUNT-RELATED TRANSCRIPTION FACTOR 1 × 1 (Q03347) CORE-BINDING FACTOR, BETA SUBUNIT × 1 (Q08024) AU GOLD ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;297 K;0.2 M potassium chloride, 0.01 M magnesium chloride, 0.01 M DTT, 4.5% V/V PEG 8000, 1% V/V glycerol, 1% V/V MPD, 0.05 M MES buffer pH 5.6, pH 5.60, VAPOR DIFFUSION, SITTING DROP, temperature 297K Resolution 3.00 Å R-free 0.299

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.

15 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CEBPB_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain A; PDBConstruct 1–78; UniProt 259–336 Author chain B; PDBConstruct 1–78; UniProt 259–336

RUNT-RELATED TRANSCRIPTION FACTOR 1

Mus musculus

UniProt Q03347

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 60–182 Fragment:RUNT DOMAIN CSF-1R PROMOTER × 1 CSF-1R PROMOTER × 1 CAAT/ENHANCER BINDING PROTEIN BETA × 2 (P17676) CORE-BINDING FACTOR, BETA SUBUNIT × 1 (Q08024) AU GOLD ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;297 K;0.2 M potassium chloride, 0.01 M magnesium chloride, 0.01 M DTT, 4.5% V/V PEG 8000, 1% V/V glycerol, 1% V/V MPD, 0.05 M MES buffer pH 5.6, pH 5.60, VAPOR DIFFUSION, SITTING DROP, temperature 297K Resolution 3.00 Å R-free 0.299

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.

17 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUNX1_MOUSE
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–123; UniProt 60–182

CORE-BINDING FACTOR, BETA SUBUNIT

Mus musculus

UniProt Q08024

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain D; UniProt 1–141 Fragment:CORE DOMAIN CSF-1R PROMOTER × 1 CSF-1R PROMOTER × 1 CAAT/ENHANCER BINDING PROTEIN BETA × 2 (P17676) RUNT-RELATED TRANSCRIPTION FACTOR 1 × 1 (Q03347) AU GOLD ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;297 K;0.2 M potassium chloride, 0.01 M magnesium chloride, 0.01 M DTT, 4.5% V/V PEG 8000, 1% V/V glycerol, 1% V/V MPD, 0.05 M MES buffer pH 5.6, pH 5.60, VAPOR DIFFUSION, SITTING DROP, temperature 297K Resolution 3.00 Å R-free 0.299

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.

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PEBB_MOUSE
Isoform
PDB entities 5
Chains and sequence ranges Author chain D; PDBConstruct 1–141; UniProt 1–141

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 1io4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1io4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1io4
Deposition date deposition_date2001-01-10
Structure title titleCRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN-CBFBETA CORE DOMAIN HETERODIMER AND C/EBPBETA BZIP HOMODIMER BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER
Keywords keywordsPROTEIN-DNA COMPLEX, TRANSCRIPTION FACTOR, BZIP, RUNX, RUNT, C/EBP, CBF, CORE BINDING FACTOR, AML1, AML, TRANSCRIPTION-DNA COMPLEX; TRANSCRIPTION/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.59
Radius of gyration Rg (electron density) rg_electron31.20
Forward intensity I(0) i087743200.00
Molecular weight molecular_weight61041.0 kDa
Excluded volume excluded_volume70804 ų
Envelope volume envelope_volume104350 ų
Hydration-shell volume shell_volume29166 ų
Envelope diameter envelope_diameter100.3
Shell Rg shell_rg36.50
Envelope Rg envelope_rg30.80
Shape Rg shape_rg31.20
Total Rg total_rg31.61
Total atoms total_atoms4189
Residues n_residues433
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 dmax99.9
Rg (real space) rg_real31.54
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real8.7740e+07
I(0) uncertainty (real space) i0_real_error1.3550e+06
Rg (reciprocal space) rg_reciprocal31.57
I(0) (reciprocal space) i0_reciprocal87740000.0000
Solution quality estimate total_estimate0.9058
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.9
Skewness Skewness skewness0.125
Kurtosis Kurtosis kurtosis-0.743
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4527000.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.954; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.942

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1io4a_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain
Domain ID domain_idd1io4b_
Class classh — Coiled coil proteins
Fold Fold foldh.1 — Parallel coiled-coil
Superfamily Superfamily superfamilyh.1.3 — Leucine zipper domain
Family Family familyh.1.3.1 — Leucine zipper domain
Domain ID domain_idd1io4c_
Class classb — All beta proteins
Fold Fold foldb.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamilyb.2.5 — p53-like transcription factors
Family Family familyb.2.5.6 — RUNT domain
Domain ID domain_idd1io4d_
Class classb — All beta proteins
Fold Fold foldb.54 — Core binding factor beta, CBF
Superfamily Superfamily superfamilyb.54.1 — Core binding factor beta, CBF
Family Family familyb.54.1.1 — Core binding factor beta, CBF

CATH v4.4 (4 domains)

Domain ID domain_id1io4A00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id1io4B00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily170
Domain ID domain_id1io4C00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily720
Domain ID domain_id1io4D00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology250 — Polyomavirus Enhancer Binding Protein 2; Chain: A;
Homologous superfamily homologous superfamily10 — Core binding factor, beta subunit

8. Citations (2)

9. Files and Curves (10)