7b92

Structure of a minimal SF3B core in complex with sudemycin D6 (form II)

Method: X-RAY DIFFRACTION Dmax: 129.6 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 1–442 Chain A; UniProt 768–1216 Not recorded 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 T2W [(~{Z},2~{S})-5-[[4-[(2~{E},4~{E})-3-methyl-5-[(2~{S},4~{R})-4,6,6-trimethyl-4-oxidanyl-oxan-2-yl]penta-2,4-dienyl]cyclohexyl]amino]-5-oxidanylidene-pent-3-en-2-yl] ~{N}-methylcarbamate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;0.1 M HEPES pH=7.42, 0.2 M Magnesium chloride, 27.75% (v/v) PEG-400 Resolution 3.00 Å R-free 0.258

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 11–452; UniProt 1–442 Author chain A; PDBConstruct 460–890; UniProt 768–1216

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 1–86 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 T2W [(~{Z},2~{S})-5-[[4-[(2~{E},4~{E})-3-methyl-5-[(2~{S},4~{R})-4,6,6-trimethyl-4-oxidanyl-oxan-2-yl]penta-2,4-dienyl]cyclohexyl]amino]-5-oxidanylidene-pent-3-en-2-yl] ~{N}-methylcarbamate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;0.1 M HEPES pH=7.42, 0.2 M Magnesium chloride, 27.75% (v/v) PEG-400 Resolution 3.00 Å R-free 0.258

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 1–86; UniProt 1–86

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 Not recorded 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 T2W [(~{Z},2~{S})-5-[[4-[(2~{E},4~{E})-3-methyl-5-[(2~{S},4~{R})-4,6,6-trimethyl-4-oxidanyl-oxan-2-yl]penta-2,4-dienyl]cyclohexyl]amino]-5-oxidanylidene-pent-3-en-2-yl] ~{N}-methylcarbamate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;0.1 M HEPES pH=7.42, 0.2 M Magnesium chloride, 27.75% (v/v) PEG-400 Resolution 3.00 Å R-free 0.258

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 Not recorded 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 T2W [(~{Z},2~{S})-5-[[4-[(2~{E},4~{E})-3-methyl-5-[(2~{S},4~{R})-4,6,6-trimethyl-4-oxidanyl-oxan-2-yl]penta-2,4-dienyl]cyclohexyl]amino]-5-oxidanylidene-pent-3-en-2-yl] ~{N}-methylcarbamate × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;277.15 K;0.1 M HEPES pH=7.42, 0.2 M Magnesium chloride, 27.75% (v/v) PEG-400 Resolution 3.00 Å R-free 0.258

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 7b92

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7b92
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7b92
Deposition date deposition_date2020-12-14
Structure title titleStructure of a minimal SF3B core in complex with sudemycin D6 (form II)
Keywords keywordsSF3B, pre-mRNA splicing, splicing modulator, sudemycin D6, SPLICING; SPLICING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier40.23
Radius of gyration Rg (electron density) rg_electron39.75
Forward intensity I(0) i0638816000.00
Molecular weight molecular_weight210550.0 kDa
Excluded volume excluded_volume265130 ų
Envelope volume envelope_volume355010 ų
Hydration-shell volume shell_volume72368 ų
Envelope diameter envelope_diameter129.8
Shell Rg shell_rg47.03
Envelope Rg envelope_rg39.22
Shape Rg shape_rg39.75
Total Rg total_rg40.11
Total atoms total_atoms14791
Residues n_residues1861
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 dmax129.6
Rg (real space) rg_real40.09
Rg uncertainty (real space) rg_real_error0.78
I(0) (real space) i0_real6.3880e+08
I(0) uncertainty (real space) i0_real_error1.0070e+07
Rg (reciprocal space) rg_reciprocal40.23
I(0) (reciprocal space) i0_reciprocal638900000.0000
Solution quality estimate total_estimate0.8959
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.8
Skewness Skewness skewness0.178
Kurtosis Kurtosis kurtosis-0.497
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha80360000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7b92A01
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_id7b92A02
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)