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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：Q92621 New Search
5PDB entries
5Biological assembly
20chain/assembly records
Main Difference Dimensions in This Set
Different assembly state Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric（208） Consistent with protein count
Chain D 1–2012（2012 aa）
Chain J 1–2012（2012 aa）
Chain P 1–2012（2012 aa）
Chain V 1–2012（2012 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 208 PDB declaration: 208-meric（208） Consistent with protein count
Chain D 1–2012（2012 aa）
Chain P 1–2012（2012 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
7PER Model of the inner ring of the human nuclear pore complex Deposited 2021-08-11 Assembly 1 Protein heterocomplex Heteromer；Protein × 192 PDB declaration: 192-meric（192） Consistent with protein count
Chain D 1–2012（2012 aa）
Chain J 1–2012（2012 aa）
Chain P 1–2012（2012 aa）
Chain V 1–2012（2012 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric（808） Consistent with protein count
Chain C0 1–2012（2012 aa）
Chain C1 1–2012（2012 aa）
Chain C2 1–2012（2012 aa）
Chain C3 1–2012（2012 aa）
Chain C4 1–2012（2012 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 Assembly 1 Protein heterocomplex Heteromer；Protein × 808 PDB declaration: 808-meric（808） Consistent with protein count
Chain C0 1–2012（2012 aa）
Chain C1 1–2012（2012 aa）
Chain C2 1–2012（2012 aa）
Chain C3 1–2012（2012 aa）
Chain C4 1–2012（2012 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

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.