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7mw1

Crystal structure of the Homo sapiens NUP93-NUP53 complex (NUP93 residues 174-819; NUP53 residues 84-150)

Method: X-RAY DIFFRACTION Dmax: 163.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Nuclear pore complex protein Nup93

Homo sapiens

UniProt Q8N1F7

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 174–819 Not recorded Nucleoporin Nup35 × 1 （Q8NFH5） X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；294 K；0.075 M TRIS pH 8.5, 17% (w/v) PEG 20000 Resolution 3.40 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 174–819 Not recorded Nucleoporin Nup35 × 1 （Q8NFH5） X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；294 K；0.075 M TRIS pH 8.5, 17% (w/v) PEG 20000 Resolution 3.40 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.

Other PDB Difference from Current Entry 7MW1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5IJN Composite structure of the inner ring of the human nuclear pore complex (32 copies of Nup205) Deposited 2016-03-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric
Chain C 1–819（819 aa）
Chain I 1–819（819 aa）
Chain O 1–819（819 aa）
Chain U 1–819（819 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 21.40 Å
5IJO Alternative composite structure of the inner ring of the human nuclear pore complex (16 copies of Nup188, 16 copies of Nup205) Deposited 2016-03-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric
Chain C 1–819（819 aa）
Chain I 1–819（819 aa）
Chain O 1–819（819 aa）
Chain U 1–819（819 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 21.40 Å
7MW0 Crystal structure of Homo sapiens NUP93 solenoid (residues 174-819) Deposited 2021-05-15 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 174–819（646 aa）
Not recorded EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；294 K；0.075 M TRIS pH 8.5, 19 % (w/v) PEG 20000
Resolution 2.00 Å R-free 0.254
7PER Model of the inner ring of the human nuclear pore complex Deposited 2021-08-11 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain C 1–819（819 aa）
Chain I 1–819（819 aa）
Chain O 1–819（819 aa）
Chain U 1–819（819 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE；Cells were grown on holey carbon, Au-mesh supports. Grids were rinsed briefly with PBS and manually blotted before plunging into liquid ethane.
Resolution 35.00 Å
7R5J Human nuclear pore complex (dilated) Deposited 2022-02-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain A0 1–819（819 aa）
Chain A1 1–819（819 aa）
Chain A2 1–819（819 aa）
Chain A3 1–819（819 aa）
Chain A4 1–819（819 aa）
Chain A5 1–819（819 aa）
Chain A6 1–819（819 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 50.00 Å
7R5K Human nuclear pore complex (constricted) Deposited 2022-02-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain A0 1–819（819 aa）
Chain A1 1–819（819 aa）
Chain A2 1–819（819 aa）
Chain A3 1–819（819 aa）
Chain A4 1–819（819 aa）
Chain A5 1–819（819 aa）
Chain A6 1–819（819 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 12.00 Å

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP93_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 27–672； UniProt 174–819 Author chain B； PDBConstruct 27–672； UniProt 174–819

Nucleoporin Nup35

Homo sapiens

UniProt Q8NFH5

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 × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain C； UniProt 84–150 Not recorded Nuclear pore complex protein Nup93 × 1 （Q8N1F7） X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；294 K；0.075 M TRIS pH 8.5, 17% (w/v) PEG 20000 Resolution 3.40 Å R-free 0.276
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain D； UniProt 84–150 Not recorded Nuclear pore complex protein Nup93 × 1 （Q8N1F7） X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 8.5；294 K；0.075 M TRIS pH 8.5, 17% (w/v) PEG 20000 Resolution 3.40 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.

Other PDB Difference from Current Entry 7MW1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4LIR Crystal structure of a nucleoporin 35kDa (NUP35) from Homo sapiens at 2.46 A resolution Deposited 2013-07-03 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 151–266（116 aa） Fragment：UNP residues 151-266
Chain B 151–266（116 aa） Fragment：UNP residues 151-266
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4；277 K；20.0% MPD, 0.1M Citrate pH 4.0, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.46 Å R-free 0.206
7R5J Human nuclear pore complex (dilated) Deposited 2022-02-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain F0 1–326（326 aa）
Chain F1 1–326（326 aa）
Chain F2 1–326（326 aa）
Chain F3 1–326（326 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 50.00 Å
7R5K Human nuclear pore complex (constricted) Deposited 2022-02-10 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain F0 1–326（326 aa）
Chain F1 1–326（326 aa）
Chain F2 1–326（326 aa）
Chain F3 1–326（326 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 12.00 Å
8OZB Crystal structure of Nup35-Nb complex Deposited 2023-05-08 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 173–248（76 aa）
Chain F 173–248（76 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.05 M HEPES (pH 6.5); 25% v/v PEG400; 0.05 M NaCl, 0.01 M MgCl2.
Resolution 2.09 Å R-free 0.267

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

View Construct and Data Evidence
UniProt name NUP35_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain C； PDBConstruct 2–68； UniProt 84–150 Author chain D； PDBConstruct 2–68； UniProt 84–150

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 7mw1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mw1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7mw1
Deposition date deposition_date2021-05-15
Structure title titleCrystal structure of the Homo sapiens NUP93-NUP53 complex (NUP93 residues 174-819; NUP53 residues 84-150)
Keywords keywordsnuclear pore complex, nucleocytoplasmic transport, alpha-helical solenoid, nuclear pore, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier46.01 Å
Radius of gyration Rg (electron density) rg_electron46.14 Å
Forward intensity I(0) i0304394000.00
Molecular weight molecular_weight144830.0 kDa
Excluded volume excluded_volume181970 ų
Envelope volume envelope_volume254190 ų
Hydration-shell volume shell_volume48612 ų
Envelope diameter envelope_diameter161.3 Å
Shell Rg shell_rg46.61 Å
Envelope Rg envelope_rg45.48 Å
Shape Rg shape_rg46.16 Å
Total Rg total_rg46.10 Å
Total atoms total_atoms20384
Residues n_residues1258
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax163.5 Å
Rg (real space) rg_real46.51 Å
Rg uncertainty (real space) rg_real_error2.30 Å
I(0) (real space) i0_real3.0440e+08
I(0) uncertainty (real space) i0_real_error6.2730e+06
Rg (reciprocal space) rg_reciprocal46.02 Å
I(0) (reciprocal space) i0_reciprocal304200000.0000
Solution quality estimate total_estimate0.7550
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary43.3 Å
Skewness Skewness skewness0.507
Kurtosis Kurtosis kurtosis-0.495
Angular range angular_range— – 0.1700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19890000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.663; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.820; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)