7evs

Crystal structure of hnRNP LL RRM2 in complex with SETD2

Method: X-RAY DIFFRACTION Dmax: 59.2 Å Quality: GOOD

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

Heterogeneous nuclear ribonucleoprotein L-like

Homo sapiens

UniProt Q8WVV9

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 166–268 Not recorded SHI domain from Histone-lysine N-methyltransferase SETD2 × 1 (Q9BYW2) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.3M Ammonium Sulfate, 20% PEG 4000 Resolution 1.60 Å R-free 0.204
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 166–268 Not recorded SHI domain from Histone-lysine N-methyltransferase SETD2 × 1 (Q9BYW2) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.3M Ammonium Sulfate, 20% PEG 4000 Resolution 1.60 Å R-free 0.204

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 HNRLL_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–110; UniProt 166–268 Author chain B; PDBConstruct 8–110; UniProt 166–268

SHI domain from Histone-lysine N-methyltransferase SETD2

OrganismNot specified

UniProt Q9BYW2

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 C; UniProt 2180–2192 Not recorded Heterogeneous nuclear ribonucleoprotein L-like × 1 (Q8WVV9) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.3M Ammonium Sulfate, 20% PEG 4000 Resolution 1.60 Å R-free 0.204
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 2180–2192 Not recorded Heterogeneous nuclear ribonucleoprotein L-like × 1 (Q8WVV9) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0.3M Ammonium Sulfate, 20% PEG 4000 Resolution 1.60 Å R-free 0.204

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.

42 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SETD2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–13; UniProt 2180–2192 Author chain D; PDBConstruct 1–13; UniProt 2180–2192

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 7evs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7evs
Deposition date deposition_date2021-05-22
Structure title titleCrystal structure of hnRNP LL RRM2 in complex with SETD2
Keywords keywordscomplex, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.48
Radius of gyration Rg (electron density) rg_electron17.18
Forward intensity I(0) i010493800.00
Molecular weight molecular_weight24694.0 kDa
Excluded volume excluded_volume31237 ų
Envelope volume envelope_volume35691 ų
Hydration-shell volume shell_volume17307 ų
Envelope diameter envelope_diameter57.1
Shell Rg shell_rg23.28
Envelope Rg envelope_rg17.39
Shape Rg shape_rg17.14
Total Rg total_rg18.31
Total atoms total_atoms1731
Residues n_residues227
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 dmax59.2
Rg (real space) rg_real18.38
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real1.0490e+07
I(0) uncertainty (real space) i0_real_error1.3080e+05
Rg (reciprocal space) rg_reciprocal18.39
I(0) (reciprocal space) i0_reciprocal10490000.0000
Solution quality estimate total_estimate0.8147
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.169
Kurtosis Kurtosis kurtosis-0.423
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1991000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)