1opi

SOLUTION STRUCTURE OF THE THIRD RNA RECOGNITION MOTIF (RRM) OF U2AF65 IN COMPLEX WITH AN N-TERMINAL SF1 PEPTIDE

Method: SOLUTION NMR Dmax: 47.1 Å Quality: GOOD

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 372–475 Fragment:C-TERMINAL RRM DOMAIN SPLICING FACTOR SF1 × 1 (Q15637) SOLUTION NMR NMR measurement conditions:pH 6.4;295 K;Ionic strength (raw mmCIF value) 50mM SALT;Pressure AMBIENT NMR sample composition:1MM 15N,13C U2AF65-RRM3 + 1MM UNLABELED SF1_10-25, 30MM PHOSPHATE BUFFER, 20MM NACL, 3MM DTT | D2O Resolution not provided

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–104; UniProt 372–475

SPLICING FACTOR SF1

OrganismNot specified

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 13–25 Fragment:N-TERMINAL PEPTIDE SPLICING FACTOR U2AF 65 KDA SUBUNIT × 1 (P26368) SOLUTION NMR NMR measurement conditions:pH 6.4;295 K;Ionic strength (raw mmCIF value) 50mM SALT;Pressure AMBIENT NMR sample composition:1MM 15N,13C U2AF65-RRM3 + 1MM UNLABELED SF1_10-25, 30MM PHOSPHATE BUFFER, 20MM NACL, 3MM DTT | D2O Resolution not provided

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 14 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 1–13; UniProt 13–25

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 1opi

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1opi
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1opi
Deposition date deposition_date2003-03-05
Structure title titleSOLUTION STRUCTURE OF THE THIRD RNA RECOGNITION MOTIF (RRM) OF U2AF65 IN COMPLEX WITH AN N-TERMINAL SF1 PEPTIDE
Keywords keywords;NON-CANONICAL RNA RECOGNITION MOTIF, 4-STRANDED ANTI-PARALLEL BETA-SHEET, 2 ALPHA HELICES ADDITIONALLY EXTENDED BY A THIRD HELIX C, RNA BINDING PROTEIN ;; RNA BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier14.50
Radius of gyration Rg (electron density) rg_electron14.07
Forward intensity I(0) i0278004000.00
Molecular weight molecular_weight136450.0 kDa
Excluded volume excluded_volume169260 ų
Envelope volume envelope_volume28898 ų
Hydration-shell volume shell_volume15307 ų
Envelope diameter envelope_diameter52.1
Shell Rg shell_rg22.01
Envelope Rg envelope_rg16.12
Shape Rg shape_rg14.08
Total Rg total_rg14.29
Total atoms total_atoms18890
Residues n_residues1170
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 dmax47.1
Rg (real space) rg_real14.41
Rg uncertainty (real space) rg_real_error0.34
I(0) (real space) i0_real2.7800e+08
I(0) uncertainty (real space) i0_real_error3.5260e+06
Rg (reciprocal space) rg_reciprocal14.42
I(0) (reciprocal space) i0_reciprocal278000000.0000
Solution quality estimate total_estimate0.8122
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary41.2
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.423
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha446000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1opia_
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

CATH v4.4 (1 domains)

Domain ID domain_id1opiA00
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)