9c0o

Crystal structure of DmCfp1 PHD finger bound to H3K4me3

Method: X-RAY DIFFRACTION Dmax: 48.4 Å Quality: GOOD

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

CXXC-type zinc finger protein 1

Drosophila melanogaster

UniProt Q9W352

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 56–119 Not recorded Histone H3.3C × 1 (Q6NXT2) DMS DIMETHYL SULFOXIDE × 1 ZN ZINC ION × 3 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;15% PEG3350, 0.01M Tris pH8.5, 0.2M Ammonium sulfate Resolution 1.53 Å R-free 0.194

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name CXXC1_DROME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–66; UniProt 56–119

Histone H3.3C

OrganismNot specified

UniProt Q6NXT2

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 D; UniProt 2–16 Non-standard monomer:Yes (specific site not provided by mmCIF) CXXC-type zinc finger protein 1 × 1 (Q9W352) DMS DIMETHYL SULFOXIDE × 1 ZN ZINC ION × 3 SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;295 K;15% PEG3350, 0.01M Tris pH8.5, 0.2M Ammonium sulfate Resolution 1.53 Å R-free 0.194

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.

22 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name H3C_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–15; UniProt 2–16

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 9c0o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9c0o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9c0o
Deposition date deposition_date2024-05-27
Structure title titleCrystal structure of DmCfp1 PHD finger bound to H3K4me3
Keywords keywordsChromatin binding protein, histone H3 reader, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier12.93
Radius of gyration Rg (electron density) rg_electron11.75
Forward intensity I(0) i02152410.00
Molecular weight molecular_weight8850.0 kDa
Excluded volume excluded_volume10502 ų
Envelope volume envelope_volume11961 ų
Hydration-shell volume shell_volume8895 ų
Envelope diameter envelope_diameter42.1
Shell Rg shell_rg17.23
Envelope Rg envelope_rg12.21
Shape Rg shape_rg11.74
Total Rg total_rg13.00
Total atoms total_atoms599
Residues n_residues71
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 dmax48.4
Rg (real space) rg_real12.87
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real2.1520e+06
I(0) uncertainty (real space) i0_real_error2.4730e+04
Rg (reciprocal space) rg_reciprocal12.87
I(0) (reciprocal space) i0_reciprocal2152000.0000
Solution quality estimate total_estimate0.8203
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary15.9
Skewness Skewness skewness0.218
Kurtosis Kurtosis kurtosis-0.244
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha332700.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.578; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.928; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (2)

9. Files and Curves (10)