3jro

NUP84-NUP145C-SEC13 edge element of the NPC lattice

Method: X-RAY DIFFRACTION Dmax: 154.2 Å Quality: REASONABLE

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

Fusion Protein of Protein Transport Protein SEC13 and Nucleoporin NUP145

Saccharomyces cerevisiae

UniProt P49687

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 714–1160 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP84 × 1 (P52891) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;295 K;1.15M sodium malonate, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 4.00 Å R-free 0.329

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 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU145_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 307–753; UniProt 714–1160

Fusion Protein of Protein Transport Protein SEC13 and Nucleoporin NUP145

Saccharomyces cerevisiae

UniProt Q04491

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–297 Non-standard monomer:Yes (specific site not provided by mmCIF) Nucleoporin NUP84 × 1 (P52891) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;295 K;1.15M sodium malonate, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 4.00 Å R-free 0.329

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.

19 other PDB entries and 26 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC13_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–297; UniProt 1–297

Nucleoporin NUP84

Saccharomyces cerevisiae

UniProt P52891

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–424 Non-standard monomer:Yes (specific site not provided by mmCIF) Fusion Protein of Protein Transport Protein SEC13 and Nucleoporin NUP145 × 1 (Q04491,P49687) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.7;295 K;1.15M sodium malonate, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 4.00 Å R-free 0.329

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 NUP84_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 3–426; UniProt 1–424

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 3jro

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3jro
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id3jro
Deposition date deposition_date2009-09-08
Structure title titleNUP84-NUP145C-SEC13 edge element of the NPC lattice
Keywords keywords;PROTEIN COMPLEX, CYTOPLASMIC VESICLE, ENDOPLASMIC RETICULUM, ER-GOLGI TRANSPORT, MEMBRANE, MRNA TRANSPORT, NUCLEAR PORE COMPLEX, NUCLEUS, PROTEIN TRANSPORT, TRANSLOCATION, TRANSPORT, WD REPEAT, AUTOCATALYTIC CLEAVAGE, HYDROLASE, PHOSPHOPROTEIN, TRANSPORT PROTEIN, STRUCTURAL PROTEIN ;; TRANSPORT PROTEIN, STRUCTURAL PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.44
Radius of gyration Rg (electron density) rg_electron46.29
Forward intensity I(0) i0219048000.00
Molecular weight molecular_weight123400.0 kDa
Excluded volume excluded_volume155100 ų
Envelope volume envelope_volume215440 ų
Hydration-shell volume shell_volume42800 ų
Envelope diameter envelope_diameter165.3
Shell Rg shell_rg44.10
Envelope Rg envelope_rg46.69
Shape Rg shape_rg46.28
Total Rg total_rg46.24
Total atoms total_atoms8671
Residues n_residues1068
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 dmax154.2
Rg (real space) rg_real46.20
Rg uncertainty (real space) rg_real_error1.72
I(0) (real space) i0_real2.1900e+08
I(0) uncertainty (real space) i0_real_error4.1040e+06
Rg (reciprocal space) rg_reciprocal45.45
I(0) (reciprocal space) i0_reciprocal218800000.0000
Solution quality estimate total_estimate0.6863
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary30.8
Skewness Skewness skewness0.569
Kurtosis Kurtosis kurtosis-0.530
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha33560000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.480; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.294; Smooth: 0.185

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3jroA01
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_id3jroC02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology3450 — Hyaluronidase domain-like
Homologous superfamily homologous superfamily20

8. Citations (1)

9. Files and Curves (10)