1jmt

X-ray Structure of a Core U2AF65/U2AF35 Heterodimer

Method: X-RAY DIFFRACTION Dmax: 57.4 Å Quality: GOOD

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

SPLICING FACTOR U2AF 35 KDA SUBUNIT

Homo sapiens

UniProt Q01081

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 43–146 Mutation:C67S SPLICING FACTOR U2AF 65 KDA SUBUNIT × 1 (P26368) HEZ HEXANE-1,6-DIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.3;277 K;PEG mme5000, sodium acetate, 1,6-hexanediol, MES, pH 5.3, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.20 Å R-free 0.238

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 U2AF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–104; UniProt 43–146

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 B; UniProt 85–112 Not recorded SPLICING FACTOR U2AF 35 KDA SUBUNIT × 1 (Q01081) HEZ HEXANE-1,6-DIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.3;277 K;PEG mme5000, sodium acetate, 1,6-hexanediol, MES, pH 5.3, VAPOR DIFFUSION, SITTING DROP, temperature 277K Resolution 2.20 Å R-free 0.238

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 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name U2AF2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–28; UniProt 85–112

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 1jmt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1jmt
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1jmt
Deposition date deposition_date2001-07-19
Structure title titleX-ray Structure of a Core U2AF65/U2AF35 Heterodimer
Keywords keywordsRRM, RNA SPLICING, PROLINE, PPII HELIX, PEPTIDE RECOGNITION, 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_guinier16.64
Radius of gyration Rg (electron density) rg_electron15.58
Forward intensity I(0) i04234970.00
Molecular weight molecular_weight14411.0 kDa
Excluded volume excluded_volume17868 ų
Envelope volume envelope_volume21215 ų
Hydration-shell volume shell_volume12170 ų
Envelope diameter envelope_diameter56.4
Shell Rg shell_rg20.66
Envelope Rg envelope_rg16.20
Shape Rg shape_rg15.52
Total Rg total_rg16.70
Total atoms total_atoms1015
Residues n_residues121
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 dmax57.4
Rg (real space) rg_real16.64
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real4.2350e+06
I(0) uncertainty (real space) i0_real_error5.4070e+04
Rg (reciprocal space) rg_reciprocal16.64
I(0) (reciprocal space) i0_reciprocal4235000.0000
Solution quality estimate total_estimate0.7504
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.6
Skewness Skewness skewness0.351
Kurtosis Kurtosis kurtosis-0.204
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha633100.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.793; Stabil: 1.000; Sysdev: 0.471; Positv: 1.000; Valcen: 0.972; Smooth: 0.989

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1jmta_
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.58.7.3 — Splicing factor U2AF subunits

CATH v4.4 (1 domains)

Domain ID domain_id1jmtA00
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)