1eao

THE RUNX1 Runt domain at 1.4A resolution: a structural switch and specifically bound chloride ions modulate DNA binding

Method: X-RAY DIFFRACTION Dmax: 85.5 Å Quality: REASONABLE

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 46–185 Fragment:RUNT DOMAIN RESIDUES 46-185 Mutation:YES BR BROMIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.4;25 % PEG 3350, 16% GLYCEROL, 130 MM NA CACODYLATE, PH 6.4 Resolution 1.40 Å R-free 0.173
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 46–185 Fragment:RUNT DOMAIN RESIDUES 46-185 Mutation:YES BR BROMIDE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:pH 6.4;25 % PEG 3350, 16% GLYCEROL, 130 MM NA CACODYLATE, PH 6.4 Resolution 1.40 Å R-free 0.173

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 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RUN1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–140; UniProt 46–185 Author chain B; PDBConstruct 1–140; UniProt 46–185

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 1eao

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1eao
Deposition date deposition_date2001-07-14
Structure title titleTHE RUNX1 Runt domain at 1.4A resolution: a structural switch and specifically bound chloride ions modulate DNA binding
Keywords keywords;TRANSCRIPTION/DNA, ACUTE MYELOID LEUKEMIA, AML, RUNX1, RUNT DOMAIN, CHLORIDE BINDING, TRANSCRIPTION FACTOR, IG FOLD, 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_guinier24.95
Radius of gyration Rg (electron density) rg_electron24.71
Forward intensity I(0) i013456000.00
Molecular weight molecular_weight27284.0 kDa
Excluded volume excluded_volume33887 ų
Envelope volume envelope_volume43782 ų
Hydration-shell volume shell_volume15942 ų
Envelope diameter envelope_diameter83.0
Shell Rg shell_rg29.74
Envelope Rg envelope_rg24.47
Shape Rg shape_rg24.73
Total Rg total_rg25.29
Total atoms total_atoms1904
Residues n_residues248
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 dmax85.5
Rg (real space) rg_real25.23
Rg uncertainty (real space) rg_real_error1.06
I(0) (real space) i0_real1.3460e+07
I(0) uncertainty (real space) i0_real_error2.2510e+05
Rg (reciprocal space) rg_reciprocal25.17
I(0) (reciprocal space) i0_reciprocal13460000.0000
Solution quality estimate total_estimate0.7025
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary20.4
Skewness Skewness skewness0.433
Kurtosis Kurtosis kurtosis-0.670
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2709000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.584; Stabil: 0.984; Sysdev: 1.000; Positv: 1.000; Valcen: 0.423; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1eaoa_
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_idd1eaob_
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

CATH v4.4 (2 domains)

Domain ID domain_id1eaoA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily720
Domain ID domain_id1eaoB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily720

8. Citations (1)

9. Files and Curves (10)