7f60

Crystal structure of auxiliary protein in complex with human nuclear protein

Method: X-RAY DIFFRACTION Dmax: 104.2 Å Quality: GOOD

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

mRNA export factor

Homo sapiens

UniProt P78406

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–368 Not recorded Nuclear pore complex protein Nup98-Nup96 × 1 (P52948) ORF6 protein × 1 (P0DTC6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;296 K;0.1m Bis-tris ph5.5,45%PEG4000 Resolution 2.85 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–368 Not recorded Nuclear pore complex protein Nup98-Nup96 × 1 (P52948) ORF6 protein × 1 (P0DTC6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;296 K;0.1m Bis-tris ph5.5,45%PEG4000 Resolution 2.85 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.

5 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAE1L_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–368; UniProt 1–368 Author chain B; PDBConstruct 1–368; UniProt 1–368

Nuclear pore complex protein Nup98-Nup96

Homo sapiens

UniProt P52948

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain D; UniProt 1–1817 Not recorded mRNA export factor × 1 (P78406) ORF6 protein × 1 (P0DTC6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;296 K;0.1m Bis-tris ph5.5,45%PEG4000 Resolution 2.85 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–1817 Not recorded mRNA export factor × 1 (P78406) ORF6 protein × 1 (P0DTC6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;296 K;0.1m Bis-tris ph5.5,45%PEG4000 Resolution 2.85 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.

20 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP98_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–1817; UniProt 1–1817 Author chain D; PDBConstruct 1–1817; UniProt 1–1817

ORF6 protein

Severe acute respiratory syndrome coronavirus 2

UniProt P0DTC6

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain E; UniProt 1–61 Not recorded mRNA export factor × 1 (P78406) Nuclear pore complex protein Nup98-Nup96 × 1 (P52948) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;296 K;0.1m Bis-tris ph5.5,45%PEG4000 Resolution 2.85 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain F; UniProt 1–61 Not recorded mRNA export factor × 1 (P78406) Nuclear pore complex protein Nup98-Nup96 × 1 (P52948) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;296 K;0.1m Bis-tris ph5.5,45%PEG4000 Resolution 2.85 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.

1 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NS6_SARS2
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–61; UniProt 1–61 Author chain F; PDBConstruct 1–61; UniProt 1–61

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 7f60

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7f60
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7f60
Deposition date deposition_date2021-06-23
Structure title titleCrystal structure of auxiliary protein in complex with human nuclear protein
Keywords keywordsimmune system, auxiliary protein, VIRAL PROTEIN; VIRAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.74
Radius of gyration Rg (electron density) rg_electron30.37
Forward intensity I(0) i0127788000.00
Molecular weight molecular_weight87485.0 kDa
Excluded volume excluded_volume108440 ų
Envelope volume envelope_volume135170 ų
Hydration-shell volume shell_volume37437 ų
Envelope diameter envelope_diameter111.3
Shell Rg shell_rg36.82
Envelope Rg envelope_rg30.57
Shape Rg shape_rg30.36
Total Rg total_rg30.95
Total atoms total_atoms6151
Residues n_residues777
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 dmax104.2
Rg (real space) rg_real30.87
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real1.2780e+08
I(0) uncertainty (real space) i0_real_error1.8460e+06
Rg (reciprocal space) rg_reciprocal30.82
I(0) (reciprocal space) i0_reciprocal127800000.0000
Solution quality estimate total_estimate0.8560
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.1
Skewness Skewness skewness0.473
Kurtosis Kurtosis kurtosis-0.342
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha58090000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.925; Smooth: 0.938

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7f60A01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase
Domain ID domain_id7f60B01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)