1hjc

CRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER

Method: X-RAY DIFFRACTION Dmax: 83.6 Å Quality: GOOD

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–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain A; UniProt 60–182 Fragment:RESIDUES 60-182 ;DNA (5'-(*GP*AP*AP*CP*TP*CP*TP*GP*TP*GP*GP* TP*TP*GP*CP*G)-3') ; × 1 ;DNA (5'-(CP*CP*GP*CP*AP*AP*CP*CP*AP*CP*AP* GP*AP*GP*TP*T)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;297 K;0.2 M AMMONIUM ACETATE, 0.15 M MAGNESIUM ACETATE, 5% W/V PEG 4000, 50 MM HEPES BUFFER, PH 7.0 AT 24 DEGREES C Resolution 2.65 Å R-free 0.263
2 Protein–DNA Monomer Protein × 1 DNA 2 PDB declaration: trimeric(3) Consistent with all polymer counts Chain D; UniProt 60–182 Fragment:RESIDUES 60-182 ;DNA (5'-(*GP*AP*AP*CP*TP*CP*TP*GP*TP*GP*GP* TP*TP*GP*CP*G)-3') ; × 1 ;DNA (5'-(CP*CP*GP*CP*AP*AP*CP*CP*AP*CP*AP* GP*AP*GP*TP*T)-3') ; × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;297 K;0.2 M AMMONIUM ACETATE, 0.15 M MAGNESIUM ACETATE, 5% W/V PEG 4000, 50 MM HEPES BUFFER, PH 7.0 AT 24 DEGREES C Resolution 2.65 Å R-free 0.263

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 AML1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–123; UniProt 60–182 Author chain D; PDBConstruct 1–123; UniProt 60–182

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 1hjc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1hjc
Deposition date deposition_date2001-01-11
Structure title titleCRYSTAL STRUCTURE OF RUNX-1/AML1/CBFALPHA RUNT DOMAIN BOUND TO A DNA FRAGMENT FROM THE CSF-1R PROMOTER
Keywords keywords;TRANSCRIPTION/DNA, PROTEIN-DNA COMPLEX, TRANSCRIPTION FACTOR, BZIP, RUNX, RUNT, C/EBP, CBF, CORE BINDING FACTOR, AML1, AML, ONCOPROTEIN, 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_guinier25.16
Radius of gyration Rg (electron density) rg_electron24.00
Forward intensity I(0) i057078100.00
Molecular weight molecular_weight45537.0 kDa
Excluded volume excluded_volume51398 ų
Envelope volume envelope_volume70198 ų
Hydration-shell volume shell_volume25316 ų
Envelope diameter envelope_diameter88.1
Shell Rg shell_rg30.14
Envelope Rg envelope_rg23.97
Shape Rg shape_rg23.94
Total Rg total_rg24.75
Total atoms total_atoms3126
Residues n_residues300
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 dmax83.6
Rg (real space) rg_real25.11
Rg uncertainty (real space) rg_real_error0.60
I(0) (real space) i0_real5.7080e+07
I(0) uncertainty (real space) i0_real_error7.8860e+05
Rg (reciprocal space) rg_reciprocal25.13
I(0) (reciprocal space) i0_reciprocal57080000.0000
Solution quality estimate total_estimate0.8829
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.2
Skewness Skewness skewness0.280
Kurtosis Kurtosis kurtosis-0.204
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3336000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.845; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1hjca_
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_idd1hjcd_
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_id1hjcA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily720
Domain ID domain_id1hjcD00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily720

8. Citations (2)

9. Files and Curves (10)