8f8z

PHF2 (PHD+JMJ) in Complex with H3 Histone N-Terminal Peptide

Method: X-RAY DIFFRACTION Dmax: 126.4 Å Quality: GOOD

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

Lysine-specific demethylase PHF2

Homo sapiens

UniProt O75151

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 1–451 Not recorded H3 N-Terminal Peptide × 1 (V9H1G0) ZN ZINC ION × 2 SO4 SULFATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.3;292 K;2.5M Ammonium Sulfate 90mM Bis-Tris Propane, pH 6.3 4% Pentaerythritol ethoxylate (3/4 EO/OH) Resolution 3.30 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–451 Not recorded H3 N-Terminal Peptide × 1 (V9H1G0) ZN ZINC ION × 2 SO4 SULFATE ION × 10 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.3;292 K;2.5M Ammonium Sulfate 90mM Bis-Tris Propane, pH 6.3 4% Pentaerythritol ethoxylate (3/4 EO/OH) Resolution 3.30 Å R-free 0.256

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.

8 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHF2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–455; UniProt 1–451 Author chain B; PDBConstruct 5–455; UniProt 1–451

H3 N-Terminal Peptide

OrganismNot specified

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 2–25 Non-standard monomer:Yes (specific site not provided by mmCIF) Lysine-specific demethylase PHF2 × 1 (O75151) ZN ZINC ION × 2 SO4 SULFATE ION × 8 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.3;292 K;2.5M Ammonium Sulfate 90mM Bis-Tris Propane, pH 6.3 4% Pentaerythritol ethoxylate (3/4 EO/OH) Resolution 3.30 Å R-free 0.256
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 2–25 Non-standard monomer:Yes (specific site not provided by mmCIF) Lysine-specific demethylase PHF2 × 1 (O75151) ZN ZINC ION × 2 SO4 SULFATE ION × 10 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.3;292 K;2.5M Ammonium Sulfate 90mM Bis-Tris Propane, pH 6.3 4% Pentaerythritol ethoxylate (3/4 EO/OH) Resolution 3.30 Å R-free 0.256

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 12 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 1–24; UniProt 2–25 Author chain F; PDBConstruct 1–24; UniProt 2–25

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 8f8z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8f8z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8f8z
Deposition date deposition_date2022-11-22
Structure title titlePHF2 (PHD+JMJ) in Complex with H3 Histone N-Terminal Peptide
Keywords keywords;Methyl-lysine binding; aromatic cage; plant homeodomain (PHD); Jumonji domain; plant homeodomain finger 2 (PHF2); histone H3 lysine 4 tri-methylation (H3K4me3), OXIDOREDUCTASE-TRANSFERASE complex ;; OXIDOREDUCTASE/TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.73
Radius of gyration Rg (electron density) rg_electron37.04
Forward intensity I(0) i0154589000.00
Molecular weight molecular_weight97357.0 kDa
Excluded volume excluded_volume120370 ų
Envelope volume envelope_volume158400 ų
Hydration-shell volume shell_volume38595 ų
Envelope diameter envelope_diameter135.6
Shell Rg shell_rg39.07
Envelope Rg envelope_rg37.24
Shape Rg shape_rg37.12
Total Rg total_rg36.88
Total atoms total_atoms6813
Residues n_residues871
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 dmax126.4
Rg (real space) rg_real37.21
Rg uncertainty (real space) rg_real_error1.13
I(0) (real space) i0_real1.5460e+08
I(0) uncertainty (real space) i0_real_error2.6090e+06
Rg (reciprocal space) rg_reciprocal36.91
I(0) (reciprocal space) i0_reciprocal154500000.0000
Solution quality estimate total_estimate0.8014
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.3
Skewness Skewness skewness0.636
Kurtosis Kurtosis kurtosis-0.136
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35240000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.716; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.657; Smooth: 0.610

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id8f8zA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id8f8zA02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily1360
Domain ID domain_id8f8zB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology120 — Jelly Rolls
Homologous superfamily homologous superfamily650 — Cupin
Domain ID domain_id8f8zB02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily1360

8. Citations (1)

9. Files and Curves (10)