6en4

SF3b core in complex with a splicing modulator

Method: X-RAY DIFFRACTION Dmax: 139.8 Å Quality: GOOD

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

Splicing factor 3B subunit 3

Homo sapiens

UniProt Q15393

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–1217 Mutation:internal deletion 1068-1085 Splicing factor 3B subunit 5 × 1 (Q9BWJ5) Splicing factor 3B subunit 1 × 1 (O75533) PHD finger-like domain-containing protein 5A × 1 (Q7RTV0) ZN ZINC ION × 3 BGZ [(2~{S},3~{S},4~{E},6~{S},7~{R},10~{R})-3,7-dimethyl-2-[(2~{E},4~{E},6~{S})-6-methyl-7-[(2~{R},3~{R})-3-[(2~{R},3~{S})-3-oxidanylpentan-2-yl]oxiran-2-yl]hepta-2,4-dien-2-yl]-7,10-bis(oxidanyl)-12-oxidanylidene-1-oxacyclododec-4-en-6-yl] ethanoate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;50 mM HEPES-NaOH, pH 7-7.4, 200 mM KCl, and 38-39% (v/v) pentaerythritol propoxylate (5/4 PO/OH) Resolution 3.08 Å R-free 0.266

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.

66 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SF3B3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–1201; UniProt 1–1217

Splicing factor 3B subunit 5

Homo sapiens

UniProt Q9BWJ5

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 2–86 Not recorded Splicing factor 3B subunit 3 × 1 (Q15393) Splicing factor 3B subunit 1 × 1 (O75533) PHD finger-like domain-containing protein 5A × 1 (Q7RTV0) ZN ZINC ION × 3 BGZ [(2~{S},3~{S},4~{E},6~{S},7~{R},10~{R})-3,7-dimethyl-2-[(2~{E},4~{E},6~{S})-6-methyl-7-[(2~{R},3~{R})-3-[(2~{R},3~{S})-3-oxidanylpentan-2-yl]oxiran-2-yl]hepta-2,4-dien-2-yl]-7,10-bis(oxidanyl)-12-oxidanylidene-1-oxacyclododec-4-en-6-yl] ethanoate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;50 mM HEPES-NaOH, pH 7-7.4, 200 mM KCl, and 38-39% (v/v) pentaerythritol propoxylate (5/4 PO/OH) Resolution 3.08 Å R-free 0.266

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.

66 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SF3B5_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–85; UniProt 2–86

Splicing factor 3B subunit 1

Homo sapiens

UniProt O75533

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 453–1304 Mutation:deletion 1-452 Splicing factor 3B subunit 3 × 1 (Q15393) Splicing factor 3B subunit 5 × 1 (Q9BWJ5) PHD finger-like domain-containing protein 5A × 1 (Q7RTV0) ZN ZINC ION × 3 BGZ [(2~{S},3~{S},4~{E},6~{S},7~{R},10~{R})-3,7-dimethyl-2-[(2~{E},4~{E},6~{S})-6-methyl-7-[(2~{R},3~{R})-3-[(2~{R},3~{S})-3-oxidanylpentan-2-yl]oxiran-2-yl]hepta-2,4-dien-2-yl]-7,10-bis(oxidanyl)-12-oxidanylidene-1-oxacyclododec-4-en-6-yl] ethanoate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;50 mM HEPES-NaOH, pH 7-7.4, 200 mM KCl, and 38-39% (v/v) pentaerythritol propoxylate (5/4 PO/OH) Resolution 3.08 Å R-free 0.266

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.

71 other PDB entries and 77 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SF3B1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–852; UniProt 453–1304

PHD finger-like domain-containing protein 5A

Homo sapiens

UniProt Q7RTV0

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 1–98 Mutation:deletion 99-110 Splicing factor 3B subunit 3 × 1 (Q15393) Splicing factor 3B subunit 5 × 1 (Q9BWJ5) Splicing factor 3B subunit 1 × 1 (O75533) ZN ZINC ION × 3 BGZ [(2~{S},3~{S},4~{E},6~{S},7~{R},10~{R})-3,7-dimethyl-2-[(2~{E},4~{E},6~{S})-6-methyl-7-[(2~{R},3~{R})-3-[(2~{R},3~{S})-3-oxidanylpentan-2-yl]oxiran-2-yl]hepta-2,4-dien-2-yl]-7,10-bis(oxidanyl)-12-oxidanylidene-1-oxacyclododec-4-en-6-yl] ethanoate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293.15 K;50 mM HEPES-NaOH, pH 7-7.4, 200 mM KCl, and 38-39% (v/v) pentaerythritol propoxylate (5/4 PO/OH) Resolution 3.08 Å R-free 0.266

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.

64 other PDB entries and 65 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PHF5A_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 11–108; UniProt 1–98

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 6en4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6en4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6en4
Deposition date deposition_date2017-10-04
Structure title titleSF3b core in complex with a splicing modulator
Keywords keywordsProtein complex, splicing modulator, SPLICING; SPLICING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier43.40
Radius of gyration Rg (electron density) rg_electron42.90
Forward intensity I(0) i0858805000.00
Molecular weight molecular_weight245530.0 kDa
Excluded volume excluded_volume309000 ų
Envelope volume envelope_volume418530 ų
Hydration-shell volume shell_volume79469 ų
Envelope diameter envelope_diameter151.0
Shell Rg shell_rg49.57
Envelope Rg envelope_rg42.27
Shape Rg shape_rg42.89
Total Rg total_rg43.22
Total atoms total_atoms17246
Residues n_residues2180
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 dmax139.8
Rg (real space) rg_real43.20
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real8.5880e+08
I(0) uncertainty (real space) i0_real_error1.4140e+07
Rg (reciprocal space) rg_reciprocal43.39
I(0) (reciprocal space) i0_reciprocal859000000.0000
Solution quality estimate total_estimate0.8981
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary54.4
Skewness Skewness skewness0.147
Kurtosis Kurtosis kurtosis-0.484
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha104400000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.905; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.967

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd6en4d_
Class classg — Small proteins
Fold Fold foldg.101 — Triquetra knot
Superfamily Superfamily superfamilyg.101.1 — Pre-mRNA splicing factor Phf5-like
Family Family familyg.101.1.1 — Pre-mRNA splicing factor Phf5-like

CATH v4.4 (2 domains)

Domain ID domain_id6en4A01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id6en4A02
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)