4cek

Crystal structure of the second MIF4G domain of human nonsense mediated decay factor UPF2

Method: X-RAY DIFFRACTION Dmax: 73.2 Å Quality: GOOD

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

REGULATOR OF NONSENSE TRANSCRIPTS 2

HOMO SAPIENS

UniProt Q9HAU5

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 455–757 Fragment:MIF4G2, RESIDUES 455-757 No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;100 MM MES PH 6.0, 19% PEG 3350 AND AT A PROTEIN CONCENTRATION OF 8 MG/ML Resolution 2.35 Å R-free 0.251

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.

5 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RENT2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–307; UniProt 455–757

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 4cek

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4cek
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4cek
Deposition date deposition_date2013-11-11
Structure title titleCrystal structure of the second MIF4G domain of human nonsense mediated decay factor UPF2
Keywords keywordsTRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.10
Radius of gyration Rg (electron density) rg_electron19.07
Forward intensity I(0) i013942000.00
Molecular weight molecular_weight28001.0 kDa
Excluded volume excluded_volume35138 ų
Envelope volume envelope_volume41707 ų
Hydration-shell volume shell_volume18582 ų
Envelope diameter envelope_diameter72.5
Shell Rg shell_rg25.15
Envelope Rg envelope_rg19.44
Shape Rg shape_rg19.05
Total Rg total_rg20.03
Total atoms total_atoms1958
Residues n_residues240
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 dmax73.2
Rg (real space) rg_real20.09
Rg uncertainty (real space) rg_real_error0.71
I(0) (real space) i0_real1.3940e+07
I(0) uncertainty (real space) i0_real_error2.1000e+05
Rg (reciprocal space) rg_reciprocal20.10
I(0) (reciprocal space) i0_reciprocal13940000.0000
Solution quality estimate total_estimate0.8409
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0
Skewness Skewness skewness0.390
Kurtosis Kurtosis kurtosis-0.123
Angular range angular_range— – 0.3950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3672000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.659; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.998

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)