7d8a

Crystal Structure of H3(1-13)/PHF14-PZP fusion protein

Method: X-RAY DIFFRACTION Dmax: 65.5 Å Quality: GOOD

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

PHD finger protein 14

Danio rerio

UniProt A0A286Y9D1

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 278–487 Fragment:PHF14-PZP Gene for histone H3 (germline gene) × 1 (V9H1G0) ZN ZINC ION × 5 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.1 M Hepes pH 7.5, 18% PEG4000, 12% isopropanol . Resolution 2.00 Å R-free 0.212

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A286Y9D1_DANRE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–210; UniProt 278–487

Gene for histone H3 (germline gene)

Homo sapiens

UniProt V9H1G0

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 E; UniProt 2–13 Fragment:H3(1-13) PHD finger protein 14 × 1 (A0A286Y9D1) ZN ZINC ION × 5 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;0.1 M Hepes pH 7.5, 18% PEG4000, 12% isopropanol . Resolution 2.00 Å R-free 0.212

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name V9H1G0_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–12; UniProt 2–13

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 7d8a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7d8a
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7d8a
Deposition date deposition_date2020-10-07
Structure title titleCrystal Structure of H3(1-13)/PHF14-PZP fusion protein
Keywords keywordsH3(1-13)/PHF14-PZP, GENE REGULATION; GENE REGULATION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.51
Radius of gyration Rg (electron density) rg_electron17.48
Forward intensity I(0) i011953200.00
Molecular weight molecular_weight23618.0 kDa
Excluded volume excluded_volume28601 ų
Envelope volume envelope_volume34639 ų
Hydration-shell volume shell_volume16807 ų
Envelope diameter envelope_diameter65.6
Shell Rg shell_rg23.42
Envelope Rg envelope_rg17.88
Shape Rg shape_rg17.50
Total Rg total_rg18.32
Total atoms total_atoms1622
Residues n_residues210
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 dmax65.5
Rg (real space) rg_real18.47
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.1950e+07
I(0) uncertainty (real space) i0_real_error1.4710e+05
Rg (reciprocal space) rg_reciprocal18.48
I(0) (reciprocal space) i0_reciprocal11950000.0000
Solution quality estimate total_estimate0.8518
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.338
Kurtosis Kurtosis kurtosis-0.109
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1692000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.697; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)