3bg1

Architecture of a Coat for the Nuclear Pore Membrane

Method: X-RAY DIFFRACTION Dmax: 220.7 Å Quality: GOOD

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

Protein SEC13 homolog

Homo sapiens

UniProt P55735

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–316 Chain D; UniProt 1–316 Chain E; UniProt 1–316 Chain H; UniProt 1–316 Not recorded Nucleoporin NUP145 × 4 (P49687) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–316 Chain D; UniProt 1–316 Not recorded Nucleoporin NUP145 × 2 (P49687) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain E; UniProt 1–316 Chain H; UniProt 1–316 Not recorded Nucleoporin NUP145 × 2 (P49687) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–316 Not recorded Nucleoporin NUP145 × 1 (P49687) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–316 Not recorded Nucleoporin NUP145 × 1 (P49687) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–316 Not recorded Nucleoporin NUP145 × 1 (P49687) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
7 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 1–316 Not recorded Nucleoporin NUP145 × 1 (P49687) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294

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 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC13_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–316; UniProt 1–316 Author chain D; PDBConstruct 1–316; UniProt 1–316 Author chain E; PDBConstruct 1–316; UniProt 1–316 Author chain H; PDBConstruct 1–316; UniProt 1–316

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 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 731–1158 Chain C; UniProt 731–1158 Chain F; UniProt 731–1158 Chain G; UniProt 731–1158 Fragment:Nucleoporin NUP145C Protein SEC13 homolog × 4 (P55735) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
2 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 731–1158 Chain C; UniProt 731–1158 Fragment:Nucleoporin NUP145C Protein SEC13 homolog × 2 (P55735) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
3 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain F; UniProt 731–1158 Chain G; UniProt 731–1158 Fragment:Nucleoporin NUP145C Protein SEC13 homolog × 2 (P55735) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 731–1158 Fragment:Nucleoporin NUP145C Protein SEC13 homolog × 1 (P55735) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 731–1158 Fragment:Nucleoporin NUP145C Protein SEC13 homolog × 1 (P55735) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 731–1158 Fragment:Nucleoporin NUP145C Protein SEC13 homolog × 1 (P55735) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294
7 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 731–1158 Fragment:Nucleoporin NUP145C Protein SEC13 homolog × 1 (P55735) X-RAY DIFFRACTION X-ray crystallization conditions:pH 7.7;294 K;16 % (w/v) PEG 3,350, 400 mM NaCl, 100 mM Na-K tartrate, and 100 mM BIS-TRIS, pH 7.7, VAPOR DIFFUSION, HANGING DROP, temperature 294K Resolution 3.00 Å R-free 0.294

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 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU145_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 15–442; UniProt 731–1158 Author chain C; PDBConstruct 15–442; UniProt 731–1158 Author chain F; PDBConstruct 15–442; UniProt 731–1158 Author chain G; PDBConstruct 15–442; UniProt 731–1158

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 3bg1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3bg1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3bg1
Deposition date deposition_date2007-11-23
Structure title titleArchitecture of a Coat for the Nuclear Pore Membrane
Keywords keywords;NPC, Transport, WD repeat, Autocatalytic cleavage, mRNA transport, Nuclear pore complex, Nucleus, Phosphoprotein, RNA-binding, Translocation, PROTEIN TRANSPORT, HYDROLASE ;; PROTEIN TRANSPORT, HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier79.98
Radius of gyration Rg (electron density) rg_electron81.78
Forward intensity I(0) i01448310000.00
Molecular weight molecular_weight320650.0 kDa
Excluded volume excluded_volume401810 ų
Envelope volume envelope_volume632040 ų
Hydration-shell volume shell_volume80485 ų
Envelope diameter envelope_diameter295.6
Shell Rg shell_rg54.18
Envelope Rg envelope_rg82.35
Shape Rg shape_rg81.79
Total Rg total_rg81.08
Total atoms total_atoms22614
Residues n_residues2822
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 dmax220.7
Rg (real space) rg_real73.31
Rg uncertainty (real space) rg_real_error1.51
I(0) (real space) i0_real1.3940e+09
I(0) uncertainty (real space) i0_real_error3.2300e+07
Rg (reciprocal space) rg_reciprocal74.13
I(0) (reciprocal space) i0_reciprocal1426000000.0000
Solution quality estimate total_estimate0.8674
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.1
Skewness Skewness skewness0.426
Kurtosis Kurtosis kurtosis-0.696
Angular range angular_range— – 0.1000 −1
Current regularization parameter α current_alpha0.0915
Highest regularization parameter α highest_alpha26870000.0000
Real-space data points n_real_points21
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.005; Oscil: 0.848; Stabil: 0.975; Sysdev: 1.000; Positv: 1.000; Valcen: 0.830; Smooth: 0.048

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 12 domains

CATH v4.4 (12 domains)

Domain ID domain_id3bg1A00
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_id3bg1B01
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology50 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily170
Domain ID domain_id3bg1B03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily690
Domain ID domain_id3bg1C01
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology50 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily170
Domain ID domain_id3bg1C03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily690
Domain ID domain_id3bg1D00
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_id3bg1E00
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_id3bg1F01
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology50 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily170
Domain ID domain_id3bg1F03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily690
Domain ID domain_id3bg1G01
Class class6 — Special
Architecture architecture20 — Other non-globular
Topology topology50 — N-terminal domain of TfIIb
Homologous superfamily homologous superfamily170
Domain ID domain_id3bg1G03
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily690
Domain ID domain_id3bg1H00
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)