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5a9q

Human nuclear pore complex

Method: ELECTRON MICROSCOPY Dmax: 747.3 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

NUCLEOPORIN NUP43

OrganismNot specified

UniProt Q8NFH3

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 × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain 0； UniProt 1–380 Chain 9； UniProt 1–380 Chain I； UniProt 1–380 Chain R； UniProt 1–380 Not recorded NUCLEAR PORE COMPLEX PROTEIN NUP160 × 32 （Q12769） NUCLEOPORIN NUP37 × 32 （Q8NFH4） NUCLEAR PORE COMPLEX PROTEIN NUP133 × 32 （Q8WUM0） NUCLEAR PORE COMPLEX PROTEIN NUP107 × 32 （P57740） NUCLEAR PORE COMPLEX PROTEIN NUP96 × 32 （P52948） PROTEIN SEC13 HOMOLOG × 32 （P55735） NUCLEOPORIN SEH1 × 32 （Q96EE3） NUCLEAR PORE COMPLEX PROTEIN NUP85 × 32 （Q9BW27） NUCLEAR PORE COMPLEX PROTEIN NUP155 × 16 （O75694） 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

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 5A9Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
4I79 Crystal structure of human NUP43 Deposited 2012-11-30 Different construct 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 1–380（380 aa）
Not recorded UNX UNKNOWN LIGAND × 13 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；291 K；25% PEG-3350, 0.1 M ammonium sulfate, 0.1 M sodium Hepes, pH 7.5, VAPOR DIFFUSION, temperature 291K
Resolution 1.75 Å R-free 0.212
4I79 Crystal structure of human NUP43 Deposited 2012-11-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–380（380 aa）
Not recorded UNX UNKNOWN LIGAND × 19 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；291 K；25% PEG-3350, 0.1 M ammonium sulfate, 0.1 M sodium Hepes, pH 7.5, VAPOR DIFFUSION, temperature 291K
Resolution 1.75 Å R-free 0.212
7PEQ Model of the outer rings of the human nuclear pore complex Deposited 2021-08-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 288 PDB declaration: 288-meric
Chain AI 1–380（380 aa）
Chain BI 1–380（380 aa）
Chain CI 1–380（380 aa）
Chain DI 1–380（380 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain Q0 1–380（380 aa）
Chain Q1 1–380（380 aa）
Chain Q2 1–380（380 aa）
Chain Q3 1–380（380 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain Q0 1–380（380 aa）
Chain Q1 1–380（380 aa）
Chain Q2 1–380（380 aa）
Chain Q3 1–380（380 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

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

View Construct and Data Evidence
UniProt name NUP43_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain 0； PDBConstruct 1–380； UniProt 1–380 Author chain 9； PDBConstruct 1–380； UniProt 1–380 Author chain I； PDBConstruct 1–380； UniProt 1–380 Author chain R； PDBConstruct 1–380； UniProt 1–380

NUCLEAR PORE COMPLEX PROTEIN NUP160

OrganismNot specified

UniProt Q12769

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 × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain 1； UniProt 1–1436 Chain J； UniProt 1–1436 Chain S； UniProt 1–1436 Chain a； UniProt 1–1436 Not recorded NUCLEOPORIN NUP43 × 32 （Q8NFH3） NUCLEOPORIN NUP37 × 32 （Q8NFH4） NUCLEAR PORE COMPLEX PROTEIN NUP133 × 32 （Q8WUM0） NUCLEAR PORE COMPLEX PROTEIN NUP107 × 32 （P57740） NUCLEAR PORE COMPLEX PROTEIN NUP96 × 32 （P52948） PROTEIN SEC13 HOMOLOG × 32 （P55735） NUCLEOPORIN SEH1 × 32 （Q96EE3） NUCLEAR PORE COMPLEX PROTEIN NUP85 × 32 （Q9BW27） NUCLEAR PORE COMPLEX PROTEIN NUP155 × 16 （O75694） 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

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 5A9Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7PEQ Model of the outer rings of the human nuclear pore complex Deposited 2021-08-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 288 PDB declaration: 288-meric
Chain AJ 1–1436（1436 aa）
Chain BJ 1–1436（1436 aa）
Chain CJ 1–1436（1436 aa）
Chain DJ 1–1436（1436 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain R0 1–1436（1436 aa）
Chain R1 1–1436（1436 aa）
Chain R2 1–1436（1436 aa）
Chain R3 1–1436（1436 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain R0 1–1436（1436 aa）
Chain R1 1–1436（1436 aa）
Chain R2 1–1436（1436 aa）
Chain R3 1–1436（1436 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

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

View Construct and Data Evidence
UniProt name NU160_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain 1； PDBConstruct 1–1436； UniProt 1–1436 Author chain J； PDBConstruct 1–1436； UniProt 1–1436 Author chain S； PDBConstruct 1–1436； UniProt 1–1436 Author chain a； PDBConstruct 1–1436； UniProt 1–1436

NUCLEOPORIN NUP37

OrganismNot specified

UniProt Q8NFH4

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 × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain 2； UniProt 1–326 Chain K； UniProt 1–326 Chain T； UniProt 1–326 Chain b； UniProt 1–326 Not recorded NUCLEOPORIN NUP43 × 32 （Q8NFH3） NUCLEAR PORE COMPLEX PROTEIN NUP160 × 32 （Q12769） NUCLEAR PORE COMPLEX PROTEIN NUP133 × 32 （Q8WUM0） NUCLEAR PORE COMPLEX PROTEIN NUP107 × 32 （P57740） NUCLEAR PORE COMPLEX PROTEIN NUP96 × 32 （P52948） PROTEIN SEC13 HOMOLOG × 32 （P55735） NUCLEOPORIN SEH1 × 32 （Q96EE3） NUCLEAR PORE COMPLEX PROTEIN NUP85 × 32 （Q9BW27） NUCLEAR PORE COMPLEX PROTEIN NUP155 × 16 （O75694） 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

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 5A9Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7PEQ Model of the outer rings of the human nuclear pore complex Deposited 2021-08-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 288 PDB declaration: 288-meric
Chain AK 1–326（326 aa）
Chain BK 1–326（326 aa）
Chain CK 1–326（326 aa）
Chain DK 1–326（326 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain S0 1–326（326 aa）
Chain S1 1–326（326 aa）
Chain S2 1–326（326 aa）
Chain S3 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain S0 1–326（326 aa）
Chain S1 1–326（326 aa）
Chain S2 1–326（326 aa）
Chain S3 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

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

View Construct and Data Evidence
UniProt name NUP37_HUMAN
Isoform —
PDB entities 3
Chains and sequence ranges Author chain 2； PDBConstruct 1–326； UniProt 1–326 Author chain K； PDBConstruct 1–326； UniProt 1–326 Author chain T； PDBConstruct 1–326； UniProt 1–326 Author chain b； PDBConstruct 1–326； UniProt 1–326

NUCLEAR PORE COMPLEX PROTEIN NUP133

OrganismNot specified

UniProt Q8WUM0

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 × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain 3； UniProt 1–1156 Chain C； UniProt 1–1156 Chain L； UniProt 1–1156 Chain U； UniProt 1–1156 Not recorded NUCLEOPORIN NUP43 × 32 （Q8NFH3） NUCLEAR PORE COMPLEX PROTEIN NUP160 × 32 （Q12769） NUCLEOPORIN NUP37 × 32 （Q8NFH4） NUCLEAR PORE COMPLEX PROTEIN NUP107 × 32 （P57740） NUCLEAR PORE COMPLEX PROTEIN NUP96 × 32 （P52948） PROTEIN SEC13 HOMOLOG × 32 （P55735） NUCLEOPORIN SEH1 × 32 （Q96EE3） NUCLEAR PORE COMPLEX PROTEIN NUP85 × 32 （Q9BW27） NUCLEAR PORE COMPLEX PROTEIN NUP155 × 16 （O75694） 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

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 5A9Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1XKS The crystal structure of the N-terminal domain of Nup133 reveals a beta-propeller fold common to several nucleoporins Deposited 2004-09-29 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 67–514（448 aa）
Mutation：F345L No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.7；277 K；PEG 3350, lithium sulfate, bis-tris, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 277.0K, pH 5.70
Resolution 2.35 Å R-free 0.236
3CQC Nucleoporin Nup107/Nup133 interaction complex Deposited 2008-04-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 935–1156（222 aa） Fragment：residues 935-1156
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；289 K；0.1M Hepes, 1.1M sodium malonate, 1-1.5% PEG MME 5000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Resolution 2.53 Å R-free 0.245
3CQG Nucleoporin Nup107/Nup133 interaction complex, delta finger mutant Deposited 2008-04-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 934–1156（223 aa） Fragment：residues 935-1156
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；289 K；25-27% PEG 2000 MME, 500mM KSCN, 0.1M Hepes, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Resolution 3.00 Å R-free 0.287
3I4R Nup107(aa658-925)/Nup133(aa517-1156) complex, H.sapiens Deposited 2009-07-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 517–1156（640 aa） Fragment：HELICAL DOMAIN (UNP residues 517-1156)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；291 K；0.8 M sodium/potassium phosphate, 15 % glycerol, 2% PEG 3350, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.53 Å R-free 0.370
7PEQ Model of the outer rings of the human nuclear pore complex Deposited 2021-08-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 288 PDB declaration: 288-meric
Chain AC 1–1156（1156 aa）
Chain BC 1–1156（1156 aa）
Chain CC 1–1156（1156 aa）
Chain DC 1–1156（1156 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain K0 1–1156（1156 aa）
Chain K1 1–1156（1156 aa）
Chain K2 1–1156（1156 aa）
Chain K3 1–1156（1156 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain K0 1–1156（1156 aa）
Chain K1 1–1156（1156 aa）
Chain K2 1–1156（1156 aa）
Chain K3 1–1156（1156 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

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NU133_HUMAN
Isoform —
PDB entities 4
Chains and sequence ranges Author chain 3； PDBConstruct 1–1156； UniProt 1–1156 Author chain C； PDBConstruct 1–1156； UniProt 1–1156 Author chain L； PDBConstruct 1–1156； UniProt 1–1156 Author chain U； PDBConstruct 1–1156； UniProt 1–1156

NUCLEAR PORE COMPLEX PROTEIN NUP107

OrganismNot specified

UniProt P57740

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 × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain 4； UniProt 1–925 Chain D； UniProt 1–925 Chain M； UniProt 1–925 Chain V； UniProt 1–925 Not recorded NUCLEOPORIN NUP43 × 32 （Q8NFH3） NUCLEAR PORE COMPLEX PROTEIN NUP160 × 32 （Q12769） NUCLEOPORIN NUP37 × 32 （Q8NFH4） NUCLEAR PORE COMPLEX PROTEIN NUP133 × 32 （Q8WUM0） NUCLEAR PORE COMPLEX PROTEIN NUP96 × 32 （P52948） PROTEIN SEC13 HOMOLOG × 32 （P55735） NUCLEOPORIN SEH1 × 32 （Q96EE3） NUCLEAR PORE COMPLEX PROTEIN NUP85 × 32 （Q9BW27） NUCLEAR PORE COMPLEX PROTEIN NUP155 × 16 （O75694） 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

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 5A9Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3CQC Nucleoporin Nup107/Nup133 interaction complex Deposited 2008-04-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 658–925（268 aa） Fragment：residues 658-925
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；289 K；0.1M Hepes, 1.1M sodium malonate, 1-1.5% PEG MME 5000, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Resolution 2.53 Å R-free 0.245
3CQG Nucleoporin Nup107/Nup133 interaction complex, delta finger mutant Deposited 2008-04-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 658–771（114 aa） Fragment：residues 658-771, 802-925, connected by linker GGSGGS
Chain A 802–925（124 aa） Fragment：residues 658-771, 802-925, connected by linker GGSGGS
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；289 K；25-27% PEG 2000 MME, 500mM KSCN, 0.1M Hepes, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 289K
Resolution 3.00 Å R-free 0.287
3I4R Nup107(aa658-925)/Nup133(aa517-1156) complex, H.sapiens Deposited 2009-07-02 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 658–925（268 aa） Fragment：C-TERMINAL FRAGMENT (UNP residues 658-925)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；291 K；0.8 M sodium/potassium phosphate, 15 % glycerol, 2% PEG 3350, pH 7.8, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 3.53 Å R-free 0.370
7PEQ Model of the outer rings of the human nuclear pore complex Deposited 2021-08-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 288 PDB declaration: 288-meric
Chain AD 1–925（925 aa）
Chain BD 1–925（925 aa）
Chain CD 1–925（925 aa）
Chain DD 1–925（925 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain L0 1–925（925 aa）
Chain L1 1–925（925 aa）
Chain L2 1–925（925 aa）
Chain L3 1–925（925 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain L0 1–925（925 aa）
Chain L1 1–925（925 aa）
Chain L2 1–925（925 aa）
Chain L3 1–925（925 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 NU107_HUMAN
Isoform —
PDB entities 5
Chains and sequence ranges Author chain 4； PDBConstruct 1–925； UniProt 1–925 Author chain D； PDBConstruct 1–925； UniProt 1–925 Author chain M； PDBConstruct 1–925； UniProt 1–925 Author chain V； PDBConstruct 1–925； UniProt 1–925

NUCLEAR PORE COMPLEX PROTEIN NUP96

OrganismNot specified

UniProt P52948

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 × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain 5； UniProt 881–1817 Chain E； UniProt 881–1817 Chain N； UniProt 881–1817 Chain W； UniProt 881–1817 Not recorded NUCLEOPORIN NUP43 × 32 （Q8NFH3） NUCLEAR PORE COMPLEX PROTEIN NUP160 × 32 （Q12769） NUCLEOPORIN NUP37 × 32 （Q8NFH4） NUCLEAR PORE COMPLEX PROTEIN NUP133 × 32 （Q8WUM0） NUCLEAR PORE COMPLEX PROTEIN NUP107 × 32 （P57740） PROTEIN SEC13 HOMOLOG × 32 （P55735） NUCLEOPORIN SEH1 × 32 （Q96EE3） NUCLEAR PORE COMPLEX PROTEIN NUP85 × 32 （Q9BW27） NUCLEAR PORE COMPLEX PROTEIN NUP155 × 16 （O75694） 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

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 5A9Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1KO6 Crystal Structure of C-terminal Autoproteolytic Domain of Nucleoporin Nup98 Deposited 2001-12-20 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 678–863（186 aa） Fragment：C-terminal Autoproteolytic Domain (Sequence database residues 677-863)
Chain B 864–920（57 aa） Fragment：C-terminal Autoproteolytic Domain (Sequence database residues 864-920)
Chain C 678–863（186 aa） Fragment：C-terminal Autoproteolytic Domain (Sequence database residues 677-863)
Chain D 864–920（57 aa） Fragment：C-terminal Autoproteolytic Domain (Sequence database residues 864-920)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.75；300 K；MgCl, PEG8000, Tris, pH 8.75, VAPOR DIFFUSION, HANGING DROP, temperature 300K
Resolution 3.00 Å R-free 0.271
2Q5X Crystal Structure of the C-terminal domain of hNup98 Deposited 2007-06-03 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 733–887（155 aa） Fragment：C-terminal domain, residues 733-887
Mutation：S881A No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.6；296 K；4.5M sodium formate, pH 4.6, vapor diffusion, hanging drop, temperature 296K
Resolution 1.90 Å R-free 0.229
2Q5Y Crystal Structure of the C-terminal domain of hNup98 Deposited 2007-06-03 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 729–880（152 aa） Fragment：C-terminal domain, residues 729-880
Chain B 881–887（7 aa） Fragment：residues 881-887
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；296 K；0.1M Tris, 0.2M MgAc2, 22% PEG8000, microseeding, pH 8.1, vapor diffusion, hanging drop, temperature 296K
Resolution 2.30 Å R-free 0.260
2Q5Y Crystal Structure of the C-terminal domain of hNup98 Deposited 2007-06-03 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 729–880（152 aa） Fragment：C-terminal domain, residues 729-880
Chain D 881–887（7 aa） Fragment：residues 881-887
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.1；296 K；0.1M Tris, 0.2M MgAc2, 22% PEG8000, microseeding, pH 8.1, vapor diffusion, hanging drop, temperature 296K
Resolution 2.30 Å R-free 0.260
3MMY Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1 Deposited 2010-04-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 158–213（56 aa） Fragment：UNP residues 158-213
Not recorded MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.65 Å R-free 0.237
3MMY Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1 Deposited 2010-04-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 158–213（56 aa） Fragment：UNP residues 158-213
Not recorded MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.65 Å R-free 0.237
3MMY Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1 Deposited 2010-04-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 158–213（56 aa） Fragment：UNP residues 158-213
Not recorded MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.65 Å R-free 0.237
3MMY Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1 Deposited 2010-04-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 158–213（56 aa） Fragment：UNP residues 158-213
Not recorded MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；VAPOR DIFFUSION, HANGING DROP
Resolution 1.65 Å R-free 0.237
4OWR Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair Rae1-Nup98 Deposited 2014-02-03 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 157–213（57 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；298 K；0.1 M HEPES pH 7.5, 11% PEG 10, 000, and 10% MPD
Resolution 3.15 Å R-free 0.289
6BZM GFGNFGTS from low-complexity/FG repeat domain of Nup98, residues 116-123 Deposited 2017-12-24 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric
Chain A 116–123（8 aa） Fragment：UNP residues 116-123
Chain B 116–123（8 aa） Fragment：UNP residues 116-123
Not recorded No recorded non-water small molecule ELECTRON CRYSTALLOGRAPHY
cryo-EM buffer pH 9.5
cryo-EM vitrification conditions Cryogen ETHANE
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；298 K；0.1 M CHES, pH 9.5, 10% ethanol
Resolution 0.90 Å R-free 0.264
7F60 Crystal structure of auxiliary protein in complex with human nuclear protein Deposited 2021-06-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 1–1817（1817 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；296 K；0.1m Bis-tris ph5.5,45%PEG4000
Resolution 2.85 Å R-free 0.276
7F60 Crystal structure of auxiliary protein in complex with human nuclear protein Deposited 2021-06-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 1–1817（1817 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；296 K；0.1m Bis-tris ph5.5,45%PEG4000
Resolution 2.85 Å R-free 0.276
7F90 Crystal structure of SARS auxiliary protein in complex with human nuclear protein Deposited 2021-07-03 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1–1817（1817 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；296 K；0.1m Bis-tris ph5.5,45%PEG4000
Resolution 2.39 Å R-free 0.258
7F90 Crystal structure of SARS auxiliary protein in complex with human nuclear protein Deposited 2021-07-03 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 1–1817（1817 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；296 K；0.1m Bis-tris ph5.5,45%PEG4000
Resolution 2.39 Å R-free 0.258
7PEQ Model of the outer rings of the human nuclear pore complex Deposited 2021-08-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 288 PDB declaration: 288-meric
Chain AE 881–1817（937 aa）
Chain BE 881–1817（937 aa）
Chain CE 881–1817（937 aa）
Chain DE 881–1817（937 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
7Q64 Cryo-em structure of the Nup98 fibril polymorph 1 Deposited 2021-11-05 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 30 PDB declaration: 30-meric
Chain A 85–124（40 aa）
Chain B 85–124（40 aa）
Chain C 85–124（40 aa）
Chain D 85–124（40 aa）
Chain E 85–124（40 aa）
Chain F 85–124（40 aa）
Chain G 85–124（40 aa）
Chain H 85–124（40 aa）
Chain I 85–124（40 aa）
Chain J 85–124（40 aa）
Chain K 85–124（40 aa）
Chain L 85–124（40 aa）
Chain M 85–124（40 aa）
Chain N 85–124（40 aa）
Chain O 85–124（40 aa）
Chain P 85–124（40 aa）
Chain Q 85–124（40 aa）
Chain R 85–124（40 aa）
Chain S 85–124（40 aa）
Chain T 85–124（40 aa）
Chain U 85–124（40 aa）
Chain V 85–124（40 aa）
Chain W 85–124（40 aa）
Chain X 85–124（40 aa）
Chain Y 85–124（40 aa）
Chain Z 85–124（40 aa）
Chain a 85–124（40 aa）
Chain b 85–124（40 aa）
Chain c 85–124（40 aa）
Chain d 85–124（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.76 Å
7Q65 Cryo-em structure of the Nup98 fibril polymorph 2 Deposited 2021-11-05 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 22 PDB declaration: 22-meric
Chain A 85–124（40 aa）
Chain B 85–124（40 aa）
Chain C 85–124（40 aa）
Chain D 85–124（40 aa）
Chain E 85–124（40 aa）
Chain F 85–124（40 aa）
Chain G 85–124（40 aa）
Chain H 85–124（40 aa）
Chain I 85–124（40 aa）
Chain J 85–124（40 aa）
Chain K 85–124（40 aa）
Chain L 85–124（40 aa）
Chain M 85–124（40 aa）
Chain N 85–124（40 aa）
Chain O 85–124（40 aa）
Chain P 85–124（40 aa）
Chain Q 85–124（40 aa）
Chain R 85–124（40 aa）
Chain S 85–124（40 aa）
Chain T 85–124（40 aa）
Chain U 85–124（40 aa）
Chain V 85–124（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.32 Å
7Q66 Cryo-em structure of the Nup98 fibril polymorph 3 Deposited 2021-11-05 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 22 PDB declaration: 22-meric
Chain A 85–124（40 aa）
Chain B 85–124（40 aa）
Chain C 85–124（40 aa）
Chain D 85–124（40 aa）
Chain E 85–124（40 aa）
Chain F 85–124（40 aa）
Chain G 85–124（40 aa）
Chain H 85–124（40 aa）
Chain I 85–124（40 aa）
Chain J 85–124（40 aa）
Chain K 85–124（40 aa）
Chain L 85–124（40 aa）
Chain M 85–124（40 aa）
Chain N 85–124（40 aa）
Chain O 85–124（40 aa）
Chain P 85–124（40 aa）
Chain Q 85–124（40 aa）
Chain R 85–124（40 aa）
Chain S 85–124（40 aa）
Chain T 85–124（40 aa）
Chain U 85–124（40 aa）
Chain V 85–124（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.79 Å
7Q67 Cryo-em structure of the Nup98 fibril polymorph 4 Deposited 2021-11-05 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 11 PDB declaration: undecameric
Chain A 85–124（40 aa）
Chain B 85–124（40 aa）
Chain C 85–124（40 aa）
Chain D 85–124（40 aa）
Chain E 85–124（40 aa）
Chain F 85–124（40 aa）
Chain G 85–124（40 aa）
Chain H 85–124（40 aa）
Chain I 85–124（40 aa）
Chain J 85–124（40 aa）
Chain K 85–124（40 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.37 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 M0 881–1817（937 aa）
Chain M1 881–1817（937 aa）
Chain M2 881–1817（937 aa）
Chain M3 881–1817（937 aa）
Chain U0 1–880（880 aa）
Chain U1 1–880（880 aa）
Chain U2 1–880（880 aa）
Chain U3 1–880（880 aa）
Chain U4 1–880（880 aa）
Chain U5 1–880（880 aa）
Chain U6 1–880（880 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 M0 881–1817（937 aa）
Chain M1 881–1817（937 aa）
Chain M2 881–1817（937 aa）
Chain M3 881–1817（937 aa）
Chain U0 1–880（880 aa）
Chain U1 1–880（880 aa）
Chain U2 1–880（880 aa）
Chain U3 1–880（880 aa）
Chain U4 1–880（880 aa）
Chain U5 1–880（880 aa）
Chain U6 1–880（880 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
7VPG Crystal structure of the C-terminal tail of SARS-CoV-1 Orf6 complex with human nucleoporin pair Rae1-Nup98 Deposited 2021-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 158–213（56 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；100 mM Sodium citrate pH 5.5, 20% PEG 3350
Resolution 2.49 Å R-free 0.231
7VPG Crystal structure of the C-terminal tail of SARS-CoV-1 Orf6 complex with human nucleoporin pair Rae1-Nup98 Deposited 2021-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 158–213（56 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；100 mM Sodium citrate pH 5.5, 20% PEG 3350
Resolution 2.49 Å R-free 0.231
7VPG Crystal structure of the C-terminal tail of SARS-CoV-1 Orf6 complex with human nucleoporin pair Rae1-Nup98 Deposited 2021-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 158–213（56 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；100 mM Sodium citrate pH 5.5, 20% PEG 3350
Resolution 2.49 Å R-free 0.231
7VPG Crystal structure of the C-terminal tail of SARS-CoV-1 Orf6 complex with human nucleoporin pair Rae1-Nup98 Deposited 2021-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain H 158–213（56 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；100 mM Sodium citrate pH 5.5, 20% PEG 3350
Resolution 2.49 Å R-free 0.231
7VPH Crystal structure of the C-terminal tail of SARS-CoV-2 Orf6 complex with human nucleoporin pair Rae1-Nup98 Deposited 2021-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 158–213（56 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；100 mM Sodium citrate pH 5.5, 20% PEG 3350
Resolution 2.80 Å R-free 0.244
7VPH Crystal structure of the C-terminal tail of SARS-CoV-2 Orf6 complex with human nucleoporin pair Rae1-Nup98 Deposited 2021-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 158–213（56 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；100 mM Sodium citrate pH 5.5, 20% PEG 3350
Resolution 2.80 Å R-free 0.244
7VPH Crystal structure of the C-terminal tail of SARS-CoV-2 Orf6 complex with human nucleoporin pair Rae1-Nup98 Deposited 2021-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain F 158–213（56 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；100 mM Sodium citrate pH 5.5, 20% PEG 3350
Resolution 2.80 Å R-free 0.244
7VPH Crystal structure of the C-terminal tail of SARS-CoV-2 Orf6 complex with human nucleoporin pair Rae1-Nup98 Deposited 2021-10-17 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain H 158–213（56 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；100 mM Sodium citrate pH 5.5, 20% PEG 3350
Resolution 2.80 Å R-free 0.244
8CI8 Cryo-EM structure of the Nup98(298-327) fibril Deposited 2023-02-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 25 PDB declaration: 25-meric
Chain A 298–327（30 aa）
Chain B 298–327（30 aa）
Chain C 298–327（30 aa）
Chain D 298–327（30 aa）
Chain E 298–327（30 aa）
Chain F 298–327（30 aa）
Chain G 298–327（30 aa）
Chain H 298–327（30 aa）
Chain I 298–327（30 aa）
Chain J 298–327（30 aa）
Chain K 298–327（30 aa）
Chain L 298–327（30 aa）
Chain M 298–327（30 aa）
Chain N 298–327（30 aa）
Chain O 298–327（30 aa）
Chain P 298–327（30 aa）
Chain Q 298–327（30 aa）
Chain R 298–327（30 aa）
Chain S 298–327（30 aa）
Chain T 298–327（30 aa）
Chain U 298–327（30 aa）
Chain V 298–327（30 aa）
Chain W 298–327（30 aa）
Chain X 298–327（30 aa）
Chain Y 298–327（30 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 6.5；In water.
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.67 Å
9PLL TRIM21-NUP98 Molecular Glue Complex (MAN-056) Deposited 2025-07-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 712–863（152 aa）
Not recorded A1BLD (3P)-3-(4-chloro-2-ethoxyphenyl)-6-fluoro-2-[(piperazin-1-yl)methyl]quinazolin-4(3H)-one × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；100 mM NaCl, 100 mM HEPES, pH 7.5, 12 % polyethylene glycol 20,000
Resolution 1.60 Å R-free 0.214
9PLM TRIM21-NUP98 Molecular Glue Complex (MAN-021) Deposited 2025-07-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 712–863（152 aa）
Not recorded A1CI1 (3P)-3-{4-chloro-2-[2-(dimethylamino)ethoxy]phenyl}-6-fluoro-2-[(piperazin-1-yl)methyl]quinazolin-4(3H)-one × 1 GOL GLYCEROL × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；100 mM NaCl, 100 mM HEPES, pH 7.5, 12 % polyethylene glycol 20,000
Resolution 1.32 Å R-free 0.178

20 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NUP98_HUMAN
Isoform —
PDB entities 6
Chains and sequence ranges Author chain 5； PDBConstruct 1–937； UniProt 881–1817 Author chain E； PDBConstruct 1–937； UniProt 881–1817 Author chain N； PDBConstruct 1–937； UniProt 881–1817 Author chain W； PDBConstruct 1–937； UniProt 881–1817

PROTEIN SEC13 HOMOLOG

OrganismNot specified

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 × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain 6； UniProt 1–322 Chain F； UniProt 1–322 Chain O； UniProt 1–322 Chain X； UniProt 1–322 Not recorded NUCLEOPORIN NUP43 × 32 （Q8NFH3） NUCLEAR PORE COMPLEX PROTEIN NUP160 × 32 （Q12769） NUCLEOPORIN NUP37 × 32 （Q8NFH4） NUCLEAR PORE COMPLEX PROTEIN NUP133 × 32 （Q8WUM0） NUCLEAR PORE COMPLEX PROTEIN NUP107 × 32 （P57740） NUCLEAR PORE COMPLEX PROTEIN NUP96 × 32 （P52948） NUCLEOPORIN SEH1 × 32 （Q96EE3） NUCLEAR PORE COMPLEX PROTEIN NUP85 × 32 （Q9BW27） NUCLEAR PORE COMPLEX PROTEIN NUP155 × 16 （O75694） 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

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 5A9Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3BG0 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–316（316 aa）
Chain D 1–316（316 aa）
Chain E 1–316（316 aa）
Chain H 1–316（316 aa）
Not recorded No recorded non-water small molecule 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 3.15 Å R-free 0.294
3BG0 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–316（316 aa）
Chain D 1–316（316 aa）
Not recorded No recorded non-water small molecule 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 3.15 Å R-free 0.294
3BG0 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 1–316（316 aa）
Chain H 1–316（316 aa）
Not recorded No recorded non-water small molecule 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 3.15 Å R-free 0.294
3BG0 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–316（316 aa）
Not recorded No recorded non-water small molecule 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 3.15 Å R-free 0.294
3BG0 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–316（316 aa）
Not recorded No recorded non-water small molecule 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 3.15 Å R-free 0.294
3BG0 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 1–316（316 aa）
Not recorded No recorded non-water small molecule 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 3.15 Å R-free 0.294
3BG0 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 1–316（316 aa）
Not recorded No recorded non-water small molecule 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 3.15 Å R-free 0.294
3BG1 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–316（316 aa）
Chain D 1–316（316 aa）
Chain E 1–316（316 aa）
Chain H 1–316（316 aa）
Not recorded No recorded non-water small molecule 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
3BG1 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–316（316 aa）
Chain D 1–316（316 aa）
Not recorded No recorded non-water small molecule 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
3BG1 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 1–316（316 aa）
Chain H 1–316（316 aa）
Not recorded No recorded non-water small molecule 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
3BG1 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–316（316 aa）
Not recorded No recorded non-water small molecule 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
3BG1 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 1–316（316 aa）
Not recorded No recorded non-water small molecule 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
3BG1 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 1–316（316 aa）
Not recorded No recorded non-water small molecule 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
3BG1 Architecture of a Coat for the Nuclear Pore Membrane Deposited 2007-11-23 Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 1–316（316 aa）
Not recorded No recorded non-water small molecule 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
7PEQ Model of the outer rings of the human nuclear pore complex Deposited 2021-08-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 288 PDB declaration: 288-meric
Chain AF 1–322（322 aa）
Chain BF 1–322（322 aa）
Chain CF 1–322（322 aa）
Chain DF 1–322（322 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain N0 1–322（322 aa）
Chain N1 1–322（322 aa）
Chain N2 1–322（322 aa）
Chain N3 1–322（322 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain N0 1–322（322 aa）
Chain N1 1–322（322 aa）
Chain N2 1–322（322 aa）
Chain N3 1–322（322 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
7UHY Human GATOR2 complex Deposited 2022-03-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain H 1–322（322 aa）
Not recorded ZN ZINC ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.66 Å
7UHY Human GATOR2 complex Deposited 2022-03-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain H 1–322（322 aa）
Not recorded ZN ZINC ION × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.66 Å
7UHY Human GATOR2 complex Deposited 2022-03-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain H 1–322（322 aa）
Not recorded ZN ZINC ION × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.66 Å
9LVJ Cryo-EM structure of Sestrin2 bound human GATOR2 complex Deposited 2025-02-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric
Chain H 1–368（368 aa）
Chain R 1–368（368 aa）
Not recorded ZN ZINC ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.82 Å
9LVK Cryo-EM structure of CASTOR1 bound human GATOR2 complex Deposited 2025-02-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric
Chain H 1–368（368 aa）
Chain R 1–368（368 aa）
Not recorded ZN ZINC ION × 31 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.59 Å
9LWF Cryo-EM structure of dual sensor bound GATOR2 complex Deposited 2025-02-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain H 1–368（368 aa）
Chain R 1–368（368 aa）
Not recorded ZN ZINC ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.41 Å
9OTI GATOR2 complex bound to arginine sensor CASTOR1 Deposited 2025-05-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric
Chain H 1–322（322 aa）
Chain R 1–322（322 aa）
Not recorded ZN ZINC ION × 29 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å

10 other PDB entries and 24 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEC13_HUMAN
Isoform —
PDB entities 7
Chains and sequence ranges Author chain 6； PDBConstruct 1–322； UniProt 1–322 Author chain F； PDBConstruct 1–322； UniProt 1–322 Author chain O； PDBConstruct 1–322； UniProt 1–322 Author chain X； PDBConstruct 1–322； UniProt 1–322

NUCLEOPORIN SEH1

OrganismNot specified

UniProt Q96EE3

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 × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain 7； UniProt 1–360 Chain G； UniProt 1–360 Chain P； UniProt 1–360 Chain Y； UniProt 1–360 Not recorded NUCLEOPORIN NUP43 × 32 （Q8NFH3） NUCLEAR PORE COMPLEX PROTEIN NUP160 × 32 （Q12769） NUCLEOPORIN NUP37 × 32 （Q8NFH4） NUCLEAR PORE COMPLEX PROTEIN NUP133 × 32 （Q8WUM0） NUCLEAR PORE COMPLEX PROTEIN NUP107 × 32 （P57740） NUCLEAR PORE COMPLEX PROTEIN NUP96 × 32 （P52948） PROTEIN SEC13 HOMOLOG × 32 （P55735） NUCLEAR PORE COMPLEX PROTEIN NUP85 × 32 （Q9BW27） NUCLEAR PORE COMPLEX PROTEIN NUP155 × 16 （O75694） 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

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 5A9Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7PEQ Model of the outer rings of the human nuclear pore complex Deposited 2021-08-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 288 PDB declaration: 288-meric
Chain AG 1–360（360 aa）
Chain BG 1–360（360 aa）
Chain CG 1–360（360 aa）
Chain DG 1–360（360 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain O0 1–360（360 aa）
Chain O1 1–360（360 aa）
Chain O2 1–360（360 aa）
Chain O3 1–360（360 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain O0 1–360（360 aa）
Chain O1 1–360（360 aa）
Chain O2 1–360（360 aa）
Chain O3 1–360（360 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
7UHY Human GATOR2 complex Deposited 2022-03-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain E 1–421（421 aa）
Chain F 1–421（421 aa）
Chain G 1–421（421 aa）
Not recorded ZN ZINC ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.66 Å
7UHY Human GATOR2 complex Deposited 2022-03-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain E 1–421（421 aa）
Chain F 1–421（421 aa）
Chain G 1–421（421 aa）
Not recorded ZN ZINC ION × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.66 Å
7UHY Human GATOR2 complex Deposited 2022-03-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain E 1–421（421 aa）
Chain F 1–421（421 aa）
Chain G 1–421（421 aa）
Not recorded ZN ZINC ION × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.66 Å
9LVJ Cryo-EM structure of Sestrin2 bound human GATOR2 complex Deposited 2025-02-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric
Chain E 1–421（421 aa）
Chain F 1–421（421 aa）
Chain G 1–421（421 aa）
Chain O 1–421（421 aa）
Chain P 1–421（421 aa）
Chain Q 1–421（421 aa）
Not recorded ZN ZINC ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.82 Å
9LVK Cryo-EM structure of CASTOR1 bound human GATOR2 complex Deposited 2025-02-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric
Chain E 1–421（421 aa）
Chain F 1–421（421 aa）
Chain G 1–421（421 aa）
Chain O 1–421（421 aa）
Chain P 1–421（421 aa）
Chain Q 1–421（421 aa）
Not recorded ZN ZINC ION × 31 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.59 Å
9LWF Cryo-EM structure of dual sensor bound GATOR2 complex Deposited 2025-02-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 20 PDB declaration: eicosameric
Chain E 1–421（421 aa）
Chain F 1–421（421 aa）
Chain G 1–421（421 aa）
Chain O 1–421（421 aa）
Chain P 1–421（421 aa）
Chain Q 1–421（421 aa）
Not recorded ZN ZINC ION × 32 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.41 Å
9OTI GATOR2 complex bound to arginine sensor CASTOR1 Deposited 2025-05-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 18 PDB declaration: octadecameric
Chain E 1–360（360 aa）
Chain F 1–360（360 aa）
Chain G 1–360（360 aa）
Chain O 1–360（360 aa）
Chain P 1–360（360 aa）
Chain Q 1–360（360 aa）
Not recorded ZN ZINC ION × 29 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å

8 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SEH1_HUMAN
Isoform —
PDB entities 8
Chains and sequence ranges Author chain 7； PDBConstruct 1–360； UniProt 1–360 Author chain G； PDBConstruct 1–360； UniProt 1–360 Author chain P； PDBConstruct 1–360； UniProt 1–360 Author chain Y； PDBConstruct 1–360； UniProt 1–360

NUCLEAR PORE COMPLEX PROTEIN NUP85

OrganismNot specified

UniProt Q9BW27

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 × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain 8； UniProt 1–656 Chain H； UniProt 1–656 Chain Q； UniProt 1–656 Chain Z； UniProt 1–656 Not recorded NUCLEOPORIN NUP43 × 32 （Q8NFH3） NUCLEAR PORE COMPLEX PROTEIN NUP160 × 32 （Q12769） NUCLEOPORIN NUP37 × 32 （Q8NFH4） NUCLEAR PORE COMPLEX PROTEIN NUP133 × 32 （Q8WUM0） NUCLEAR PORE COMPLEX PROTEIN NUP107 × 32 （P57740） NUCLEAR PORE COMPLEX PROTEIN NUP96 × 32 （P52948） PROTEIN SEC13 HOMOLOG × 32 （P55735） NUCLEOPORIN SEH1 × 32 （Q96EE3） NUCLEAR PORE COMPLEX PROTEIN NUP155 × 16 （O75694） 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

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 5A9Q Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7PEQ Model of the outer rings of the human nuclear pore complex Deposited 2021-08-11 Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 288 PDB declaration: 288-meric
Chain AH 1–656（656 aa）
Chain BH 1–656（656 aa）
Chain CH 1–656（656 aa）
Chain DH 1–656（656 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain P0 1–656（656 aa）
Chain P1 1–656（656 aa）
Chain P2 1–656（656 aa）
Chain P3 1–656（656 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 oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric
Chain P0 1–656（656 aa）
Chain P1 1–656（656 aa）
Chain P2 1–656（656 aa）
Chain P3 1–656（656 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

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

View Construct and Data Evidence
UniProt name NUP85_HUMAN
Isoform —
PDB entities 9
Chains and sequence ranges Author chain 8； PDBConstruct 1–656； UniProt 1–656 Author chain H； PDBConstruct 1–656； UniProt 1–656 Author chain Q； PDBConstruct 1–656； UniProt 1–656 Author chain Z； PDBConstruct 1–656； UniProt 1–656

NUCLEAR PORE COMPLEX PROTEIN NUP155

OrganismNot specified

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 Protein heterocomplex Heteromer Protein × 304 PDB declaration: 304-meric（304） Consistent with protein copy count Chain A； UniProt 1–1391 Chain B； UniProt 1–1391 Not recorded NUCLEOPORIN NUP43 × 32 （Q8NFH3） NUCLEAR PORE COMPLEX PROTEIN NUP160 × 32 （Q12769） NUCLEOPORIN NUP37 × 32 （Q8NFH4） NUCLEAR PORE COMPLEX PROTEIN NUP133 × 32 （Q8WUM0） NUCLEAR PORE COMPLEX PROTEIN NUP107 × 32 （P57740） NUCLEAR PORE COMPLEX PROTEIN NUP96 × 32 （P52948） PROTEIN SEC13 HOMOLOG × 32 （P55735） NUCLEOPORIN SEH1 × 32 （Q96EE3） NUCLEAR PORE COMPLEX PROTEIN NUP85 × 32 （Q9BW27） 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

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 5A9Q 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 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 mutation/modification Different oligomeric state Different experimental conditions 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 mutation/modification Different oligomeric state Different experimental conditions 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
7EYQ Cryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-1069) at 5.4 Angstrom resolution Deposited 2021-05-31 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–1391（1391 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 5.40 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 mutation/modification 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 10
Chains and sequence ranges Author chain A； PDBConstruct 1–1391； UniProt 1–1391 Author chain B； PDBConstruct 1–1391； 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 5a9q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5a9q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5a9q
Deposition date deposition_date2015-07-22
Structure title titleHuman nuclear pore complex
Keywords keywordsTRANSPORT PROTEIN; TRANSPORT 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_guinier— Å
Radius of gyration Rg (electron density) rg_electron287.20 Å
Forward intensity I(0) i036339400000.00
Molecular weight molecular_weight1341900.0 kDa
Excluded volume excluded_volume1546800 ų
Envelope volume envelope_volume11743000 ų
Hydration-shell volume shell_volume357540 ų
Envelope diameter envelope_diameter816.4 Å
Shell Rg shell_rg259.70 Å
Envelope Rg envelope_rg246.90 Å
Shape Rg shape_rg287.20 Å
Total Rg total_rg287.30 Å
Total atoms total_atoms95884
Residues n_residues19350
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 dmax747.3 Å
Rg (real space) rg_real253.00 Å
Rg uncertainty (real space) rg_real_error6.36 Å
I(0) (real space) i0_real3.2170e+10
I(0) uncertainty (real space) i0_real_error1.1200e+09
Rg (reciprocal space) rg_reciprocal136.60 Å
I(0) (reciprocal space) i0_reciprocal23680000000.0000
Solution quality estimate total_estimate0.7651
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary149.5 Å
Skewness Skewness skewness0.681
Kurtosis Kurtosis kurtosis-0.963
Angular range angular_range— – 0.0250 Å−1
Current regularization parameter α current_alpha0.6618
Highest regularization parameter α highest_alpha1603000000.0000
Real-space data points n_real_points6
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 22.340; Oscil: 0.533; Stabil: 0.808; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (10)

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8. Citations (1)

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9. Files and Curves (10)