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7eyq

Cryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-1069) at 5.4 Angstrom resolution

Method: ELECTRON MICROSCOPY Dmax: 122.7 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

G protein/GFP fusion protein,Nuclear pore complex protein Nup155

Homo sapiens

UniProt B7UCZ6

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 Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 512–750 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；Buffer was freshly made. cryo-EM vitrification conditions：Cryogen ETHANE；Blot for 3 seconds before plunging Resolution 5.40 Å

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 7EYQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6ZQO EYFP mutant - F165G Deposited 2020-07-10 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 512–750（239 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；5.7 mg/ml in 20mM Tris 8.0 200 mM NaCl mixed with a 1.44M (NH4)2SO4, 60mM Bicine pH 9.0 reservoir solution.
Resolution 2.20 Å R-free 0.340
7EYE Cryo-EM (SPA) structure of Nup155 N-terminus (19-863) at 5.1 Angstrom resolution Deposited 2021-05-30 Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 512–750（239 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；Buffer was freshly made.
cryo-EM vitrification conditions Cryogen ETHANE；Blot for 3 seconds before plunging
Resolution 5.10 Å
7FBS structure of a channel Deposited 2021-07-12 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 512–750（239 aa）
Mutation：I1487Q,F1488Q,M1489Q NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 11 4Y4 1-[2-[(2R)-2-oxidanyl-3-(propylamino)propoxy]phenyl]-3-phenyl-propan-1-one × 1 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 6
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
7XSU Cardiac sodium channel in complex with LqhIII Deposited 2022-05-15 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 512–750（239 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 BMA beta-D-mannopyranose × 1 6OU [(2~{R})-1-[2-azanylethoxy(oxidanyl)phosphoryl]oxy-3-hexadecanoyloxy-propan-2-yl] (~{Z})-octadec-9-enoate × 6 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.1
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9NTM SPEF1 bound to 14-pf microtubule Deposited 2025-03-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 89 PDB declaration: 89-meric
Chain 1A 512–750（239 aa）
Chain 1B 512–750（239 aa）
Chain 1C 512–750（239 aa）
Chain 1D 512–750（239 aa）
Chain 1E 512–750（239 aa）
Not recorded GTP GUANOSINE-5'-TRIPHOSPHATE × 42 MG MAGNESIUM ION × 42 GDP GUANOSINE-5'-DIPHOSPHATE × 42 TA1 TAXOL × 42 ELECTRON MICROSCOPY
cryo-EM buffer pH 6.8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 7.10 Å

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

View Construct and Data Evidence
UniProt name B7UCZ6_9RHAB
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–239； UniProt 512–750

G protein/GFP fusion protein,Nuclear pore complex protein Nup155

Homo sapiens

UniProt O75694

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 Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count Chain A； UniProt 1–1391 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；Buffer was freshly made. cryo-EM vitrification conditions：Cryogen ETHANE；Blot for 3 seconds before plunging Resolution 5.40 Å

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 7EYQ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
5A9Q Human nuclear pore complex Deposited 2015-07-22 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 304 PDB declaration: 304-meric
Chain A 1–1391（1391 aa）
Chain B 1–1391（1391 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20MM TRIS, 0.2-0.4% TREHALOSE；pH 7.5；20MM TRIS, 0.2-0.4% TREHALOSE
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE；VITRIFICATION 1 -- CRYOGEN- ETHANE-PROPANE MIXTURE, INSTRUMENT- HOMEMADE PLUNGER,
Resolution 23.00 Å
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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric
Chain A 1–1391（1391 aa）
Chain B 1–1391（1391 aa）
Chain E 1–1391（1391 aa）
Chain K 1–1391（1391 aa）
Chain Q 1–1391（1391 aa）
Chain W 1–1391（1391 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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric
Chain A 1–1391（1391 aa）
Chain B 1–1391（1391 aa）
Chain E 1–1391（1391 aa）
Chain K 1–1391（1391 aa）
Chain Q 1–1391（1391 aa）
Chain W 1–1391（1391 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
7EYE Cryo-EM (SPA) structure of Nup155 N-terminus (19-863) at 5.1 Angstrom resolution Deposited 2021-05-30 Different construct Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–863（863 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；Buffer was freshly made.
cryo-EM vitrification conditions Cryogen ETHANE；Blot for 3 seconds before plunging
Resolution 5.10 Å
7EYF Cryo-EM (SPA) structure of human Nup155 C-terminus (864-1337) at 5.3 Angstroms resolution Deposited 2021-05-30 Different construct Different oligomeric state Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 864–1391（528 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；Buffer was freshly made.
cryo-EM vitrification conditions Cryogen ETHANE；Blot for 3 seconds before plunging
Resolution 5.30 Å
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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric
Chain E 1–1391（1391 aa）
Chain K 1–1391（1391 aa）
Chain Q 1–1391（1391 aa）
Chain W 1–1391（1391 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
7R1Y cryoEM structure of human Nup155 (residues 19-981) Deposited 2022-02-03 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–1391（1390 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
7R5J Human nuclear pore complex (dilated) Deposited 2022-02-10 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain D0 1–1391（1391 aa）
Chain D1 1–1391（1391 aa）
Chain D2 1–1391（1391 aa）
Chain D3 1–1391（1391 aa）
Chain D4 1–1391（1391 aa）
Chain D5 1–1391（1391 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 conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain D0 1–1391（1391 aa）
Chain D1 1–1391（1391 aa）
Chain D2 1–1391（1391 aa）
Chain D3 1–1391（1391 aa）
Chain D4 1–1391（1391 aa）
Chain D5 1–1391（1391 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

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU155_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 252–1642； UniProt 1–1391

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 7eyq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7eyq
Deposition date deposition_date2021-05-31
Structure title titleCryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-1069) at 5.4 Angstrom resolution
Keywords keywordsHuman Nucleoporin, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier35.31 Å
Radius of gyration Rg (electron density) rg_electron35.42 Å
Forward intensity I(0) i0134365000.00
Molecular weight molecular_weight93587.0 kDa
Excluded volume excluded_volume117630 ų
Envelope volume envelope_volume156920 ų
Hydration-shell volume shell_volume38365 ų
Envelope diameter envelope_diameter131.6 Å
Shell Rg shell_rg39.52 Å
Envelope Rg envelope_rg36.13 Å
Shape Rg shape_rg35.45 Å
Total Rg total_rg35.65 Å
Total atoms total_atoms6577
Residues n_residues833
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 dmax122.7 Å
Rg (real space) rg_real35.61 Å
Rg uncertainty (real space) rg_real_error1.16 Å
I(0) (real space) i0_real1.3440e+08
I(0) uncertainty (real space) i0_real_error2.2380e+06
Rg (reciprocal space) rg_reciprocal35.42 Å
I(0) (reciprocal space) i0_reciprocal134300000.0000
Solution quality estimate total_estimate0.8327
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.7 Å
Skewness Skewness skewness0.569
Kurtosis Kurtosis kurtosis-0.192
Angular range angular_range— – 0.2250 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24860000.0000
Real-space data points n_real_points46
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: 0.828; Smooth: 0.732
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)