4c31

Nup1:Sac3:Sus1 complex

Method: X-RAY DIFFRACTION Dmax: 62.3 Å Quality: EXCELLENT

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

NUCLEAR MRNA EXPORT PROTEIN SAC3

SACCHAROMYCES CEREVISIAE

UniProt P46674

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 757–787 Chain D; UniProt 757–787 Fragment:RESIDUES 757-787 PROTEIN SUS1 × 2 (Q6WNK7) NUCLEOPORIN NUP1 × 4 (P20676) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;DESCRIBED IN DETAIL IN PUBLICATION, pH 6.0 Resolution 3.00 Å R-free 0.243

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 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAC3_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–33; UniProt 757–787 Author chain D; PDBConstruct 3–33; UniProt 757–787

PROTEIN SUS1

SACCHAROMYCES CEREVISIAE

UniProt Q6WNK7

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 1–96 Chain E; UniProt 1–96 Not recorded NUCLEAR MRNA EXPORT PROTEIN SAC3 × 2 (P46674) NUCLEOPORIN NUP1 × 4 (P20676) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;DESCRIBED IN DETAIL IN PUBLICATION, pH 6.0 Resolution 3.00 Å R-free 0.243

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.

15 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SUS1_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–96; UniProt 1–96 Author chain E; PDBConstruct 1–96; UniProt 1–96

NUCLEOPORIN NUP1

SACCHAROMYCES CEREVISIAE

UniProt P20676

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 C; UniProt 322–355 Chain F; UniProt 322–355 Chain X; UniProt 322–355 Chain Y; UniProt 322–355 Fragment:RESIDUES 322-355 NUCLEAR MRNA EXPORT PROTEIN SAC3 × 2 (P46674) PROTEIN SUS1 × 2 (Q6WNK7) X-RAY DIFFRACTION X-ray crystallization conditions:pH 6;DESCRIBED IN DETAIL IN PUBLICATION, pH 6.0 Resolution 3.00 Å R-free 0.243

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.

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP1_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 3–36; UniProt 322–355 Author chain F; PDBConstruct 3–36; UniProt 322–355 Author chain X; PDBConstruct 3–36; UniProt 322–355 Author chain Y; PDBConstruct 3–36; UniProt 322–355

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 4c31

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4c31
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4c31
Deposition date deposition_date2013-08-21
Structure title titleNup1:Sac3:Sus1 complex
Keywords keywordsTRANSPORT PROTEIN, NUCLEAR TRANSPORT, MRNA EXPORT, GENE EXPRESSION PATHWAY INTEGRATION, NUCLEAR PORE; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.49
Radius of gyration Rg (electron density) rg_electron20.10
Forward intensity I(0) i018457400.00
Molecular weight molecular_weight33278.0 kDa
Excluded volume excluded_volume41996 ų
Envelope volume envelope_volume50500 ų
Hydration-shell volume shell_volume20953 ų
Envelope diameter envelope_diameter64.3
Shell Rg shell_rg26.53
Envelope Rg envelope_rg20.14
Shape Rg shape_rg20.06
Total Rg total_rg21.12
Total atoms total_atoms2340
Residues n_residues286
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 dmax62.3
Rg (real space) rg_real21.36
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real1.8460e+07
I(0) uncertainty (real space) i0_real_error2.0440e+05
Rg (reciprocal space) rg_reciprocal21.38
I(0) (reciprocal space) i0_reciprocal18460000.0000
Solution quality estimate total_estimate0.9172
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.101
Kurtosis Kurtosis kurtosis-0.642
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5963000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.980; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4c31b_
Class classa — All alpha proteins
Fold Fold folda.301 — Sus1-like
Superfamily Superfamily superfamilya.301.1 — Sus1-like
Family Family familya.301.1.1 — Sus1-like
Domain ID domain_idd4c31e_
Class classa — All alpha proteins
Fold Fold folda.301 — Sus1-like
Superfamily Superfamily superfamilya.301.1 — Sus1-like
Family Family familya.301.1.1 — Sus1-like

CATH v4.4 (2 domains)

Domain ID domain_id4c31B00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily140 — ENY2/SUS1
Domain ID domain_id4c31E00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology246 — Serum Albumin; Chain A, Domain 1
Homologous superfamily homologous superfamily140 — ENY2/SUS1

8. Citations (1)

9. Files and Curves (10)