9qwn

Human UPF1 in complex with the histone stem loop RNA

Method: ELECTRON MICROSCOPY Dmax: 93.5 Å Quality: EXCELLENT

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

Isoform 2 of Regulator of nonsense transcripts 1

Homo sapiens

UniProt Q92900

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–RNA Monomer Protein × 1 RNA 1 PDB declaration: dimeric(2) Consistent with all polymer counts Chain A; UniProt 115–914 Not recorded RNA stem loop × 1 ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 Å

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.

11 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RENT1_HUMAN
Isoform Q92900-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–800; UniProt 115–914

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 9qwn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qwn
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9qwn
Deposition date deposition_date2025-04-14
Structure title titleHuman UPF1 in complex with the histone stem loop RNA
Keywords keywordsATP-DEPENDENT HELICASE RENT1, UP-FRAMESHIFT SUPPRESSOR 1 HOMOLOG, HUPF1, UP FRAMESHIFT, histone stem loop mRNA, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier30.27
Radius of gyration Rg (electron density) rg_electron29.37
Forward intensity I(0) i0170405000.00
Molecular weight molecular_weight97800.0 kDa
Excluded volume excluded_volume120080 ų
Envelope volume envelope_volume152760 ų
Hydration-shell volume shell_volume42301 ų
Envelope diameter envelope_diameter98.8
Shell Rg shell_rg37.45
Envelope Rg envelope_rg29.24
Shape Rg shape_rg29.36
Total Rg total_rg30.09
Total atoms total_atoms6825
Residues n_residues823
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 dmax93.5
Rg (real space) rg_real30.12
Rg uncertainty (real space) rg_real_error0.44
I(0) (real space) i0_real1.7040e+08
I(0) uncertainty (real space) i0_real_error2.3650e+06
Rg (reciprocal space) rg_reciprocal30.19
I(0) (reciprocal space) i0_reciprocal170400000.0000
Solution quality estimate total_estimate0.9036
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary36.0
Skewness Skewness skewness0.173
Kurtosis Kurtosis kurtosis-0.498
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26220000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)