1xk5

Crystal structure of the m3G-cap-binding domain of snurportin1 in complex with a m3GpppG-cap dinucleotide

Method: X-RAY DIFFRACTION Dmax: 60.0 Å Quality: GOOD

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

snurportin-1

Homo sapiens

UniProt O95149

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 97–300 Fragment:m3G-cap-binding domain comprising amino acids 97-300 TPG 2,2,7-TRIMETHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-GUANOSINE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;8% PEG20K, 100mM MES pH6.0 for initial crystals and 200mM sodium citrate pH5.5 for larger crystals after seeding, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 2.40 Å R-free 0.276

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.

10 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O95149_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–204; UniProt 97–300

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 1xk5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1xk5
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id1xk5
Deposition date deposition_date2004-09-27
Structure title titleCrystal structure of the m3G-cap-binding domain of snurportin1 in complex with a m3GpppG-cap dinucleotide
Keywords keywordsProtein-RNA-complex, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.17
Radius of gyration Rg (electron density) rg_electron16.99
Forward intensity I(0) i010528000.00
Molecular weight molecular_weight23956.0 kDa
Excluded volume excluded_volume29856 ų
Envelope volume envelope_volume33639 ų
Hydration-shell volume shell_volume16690 ų
Envelope diameter envelope_diameter60.9
Shell Rg shell_rg23.05
Envelope Rg envelope_rg17.29
Shape Rg shape_rg16.97
Total Rg total_rg18.00
Total atoms total_atoms1683
Residues n_residues204
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 dmax60.0
Rg (real space) rg_real18.10
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.0530e+07
I(0) uncertainty (real space) i0_real_error1.2940e+05
Rg (reciprocal space) rg_reciprocal18.11
I(0) (reciprocal space) i0_reciprocal10530000.0000
Solution quality estimate total_estimate0.8760
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.282
Kurtosis Kurtosis kurtosis-0.224
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2177000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.797; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1xk5a_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.142 — ATP-grasp
Superfamily Superfamily superfamilyd.142.2 — DNA ligase/mRNA capping enzyme, catalytic domain
Family Family familyd.142.2.5 — m3G-cap binding domain of snurportin-1

CATH v4.4 (1 domains)

Domain ID domain_id1xk5A01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily30 — DNA ligase/mRNA capping enzyme

8. Citations (3)

9. Files and Curves (10)