4fxw

Structure of phosphorylated SF1 complex with U2AF65-UHM domain

Method: X-RAY DIFFRACTION Dmax: 108.2 Å Quality: REASONABLE

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

Splicing factor U2AF 65 kDa subunit

Homo sapiens

UniProt P26368

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 375–475 Non-standard monomer:Yes (specific site not provided by mmCIF) Splicing factor 1 × 1 (Q15637) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;0.2 M Lithium sulfate, 20% PEG 3350 and 0.1 M Tris pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.29 Å R-free 0.281
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 375–475 Non-standard monomer:Yes (specific site not provided by mmCIF) Splicing factor 1 × 1 (Q15637) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;0.2 M Lithium sulfate, 20% PEG 3350 and 0.1 M Tris pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.29 Å R-free 0.281

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.

39 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name U2AF2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–106; UniProt 375–475 Author chain C; PDBConstruct 6–106; UniProt 375–475

Splicing factor 1

Homo sapiens

UniProt Q15637

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 14–132 Non-standard monomer:Yes (specific site not provided by mmCIF) Splicing factor U2AF 65 kDa subunit × 1 (P26368) SO4 SULFATE ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;0.2 M Lithium sulfate, 20% PEG 3350 and 0.1 M Tris pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.29 Å R-free 0.281
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 14–132 Non-standard monomer:Yes (specific site not provided by mmCIF) Splicing factor U2AF 65 kDa subunit × 1 (P26368) SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;0.2 M Lithium sulfate, 20% PEG 3350 and 0.1 M Tris pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 2.29 Å R-free 0.281

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 SF01_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 6–124; UniProt 14–132 Author chain D; PDBConstruct 6–124; UniProt 14–132

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 4fxw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4fxw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4fxw
Deposition date deposition_date2012-07-03
Structure title titleStructure of phosphorylated SF1 complex with U2AF65-UHM domain
Keywords keywordsUHM, pre-mRNA splicing factor, protein binding, phosphorylation; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.72
Radius of gyration Rg (electron density) rg_electron29.35
Forward intensity I(0) i042237100.00
Molecular weight molecular_weight47439.0 kDa
Excluded volume excluded_volume57936 ų
Envelope volume envelope_volume81913 ų
Hydration-shell volume shell_volume25126 ų
Envelope diameter envelope_diameter112.8
Shell Rg shell_rg33.74
Envelope Rg envelope_rg29.65
Shape Rg shape_rg29.42
Total Rg total_rg29.60
Total atoms total_atoms3288
Residues n_residues403
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 dmax108.2
Rg (real space) rg_real31.63
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real4.2590e+07
I(0) uncertainty (real space) i0_real_error5.6150e+05
Rg (reciprocal space) rg_reciprocal29.90
I(0) (reciprocal space) i0_reciprocal42230000.0000
Solution quality estimate total_estimate0.5884
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary26.5
Skewness Skewness skewness0.619
Kurtosis Kurtosis kurtosis-0.200
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha3.4650
Highest regularization parameter α highest_alpha7233000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.665; Stabil: 0.866; Sysdev: 0.000; Positv: 1.000; Valcen: 0.555; Smooth: 0.544

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4fxwa1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.1 — Canonical RBD
Domain ID domain_idd4fxwa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4fxwc1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.58 — Ferredoxin-like
Superfamily Superfamily superfamilyd.58.7 — RNA-binding domain, RBD, aka RNA recognition motif (RRM)
Family Family familyd.58.7.1 — Canonical RBD
Domain ID domain_idd4fxwc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id4fxwA00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain
Domain ID domain_id4fxwC00
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology70 — Alpha-Beta Plaits
Homologous superfamily homologous superfamily330 — RRM (RNA recognition motif) domain

8. Citations (1)

9. Files and Curves (10)