8jwj

PHD Finger Protein 7 (PHF7) in complex with UBE2D2

Method: X-RAY DIFFRACTION Dmax: 131.9 Å Quality: GOOD

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

PHD finger protein 7

Mus musculus

UniProt Q9DAG9

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 28–307 Not recorded Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) ZN ZINC ION × 7 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.3;277 K;MPD, Tris Resolution 2.96 Å R-free 0.222
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 28–307 Not recorded Ubiquitin-conjugating enzyme E2 D2 × 1 (P62837) ZN ZINC ION × 7 SO4 SULFATE ION × 1 GOL GLYCEROL × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.3;277 K;MPD, Tris Resolution 2.96 Å R-free 0.222

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.

3 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHF7_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–285; UniProt 28–307 Author chain C; PDBConstruct 6–285; UniProt 28–307

Ubiquitin-conjugating enzyme E2 D2

Homo sapiens

UniProt P62837

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 B; UniProt 1–147 Mutation:S22R, C85K PHD finger protein 7 × 1 (Q9DAG9) ZN ZINC ION × 7 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.3;277 K;MPD, Tris Resolution 2.96 Å R-free 0.222
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–147 Mutation:S22R, C85K PHD finger protein 7 × 1 (Q9DAG9) ZN ZINC ION × 7 SO4 SULFATE ION × 1 GOL GLYCEROL × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.3;277 K;MPD, Tris Resolution 2.96 Å R-free 0.222

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.

57 other PDB entries and 91 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UB2D2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–152; UniProt 1–147 Author chain D; PDBConstruct 6–152; UniProt 1–147

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 8jwj

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8jwj
Deposition date deposition_date2023-06-29
Structure title titlePHD Finger Protein 7 (PHF7) in complex with UBE2D2
Keywords keywordsUbiquitin, RING ligase, PHD, complex, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.95
Radius of gyration Rg (electron density) rg_electron37.55
Forward intensity I(0) i0158250000.00
Molecular weight molecular_weight96454.0 kDa
Excluded volume excluded_volume118570 ų
Envelope volume envelope_volume167630 ų
Hydration-shell volume shell_volume39375 ų
Envelope diameter envelope_diameter134.4
Shell Rg shell_rg40.99
Envelope Rg envelope_rg37.05
Shape Rg shape_rg37.45
Total Rg total_rg38.10
Total atoms total_atoms6694
Residues n_residues839
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 dmax131.9
Rg (real space) rg_real38.13
Rg uncertainty (real space) rg_real_error1.70
I(0) (real space) i0_real1.5820e+08
I(0) uncertainty (real space) i0_real_error3.1420e+06
Rg (reciprocal space) rg_reciprocal38.02
I(0) (reciprocal space) i0_reciprocal158200000.0000
Solution quality estimate total_estimate0.8314
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.4
Skewness Skewness skewness0.400
Kurtosis Kurtosis kurtosis-0.193
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14400000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.687; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.934; Smooth: 0.810

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)