← Back to search

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：D3Z7H4 New Search
4PDB entries
4Biological assembly
16chain/assembly records
Main Difference Dimensions in This Set
Different mutation/modification Different ligand/ion 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
5WEK GluA2 bound to antagonist ZK and GSG1L in digitonin, state 1 Deposited 2017-07-10 Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 2–238（237 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Chain B 2–238（237 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Chain C 2–238（237 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Chain D 2–238（237 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.60 Å
5WEL GluA2 bound to antagonist ZK and GSG1L in digitonin, state 2 Deposited 2017-07-10 Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 2–238（237 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Chain B 2–238（237 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Chain C 2–238（237 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Chain D 2–238（237 aa） Fragment：UNP P19491 residues 25-847, UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L ZK1 {[7-morpholin-4-yl-2,3-dioxo-6-(trifluoromethyl)-3,4-dihydroquinoxalin-1(2H)-yl]methyl}phosphonic acid × 4 AJP Digitonin × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.40 Å
5WEM GluA2 bound to GSG1L in digitonin, state 1 Deposited 2017-07-10 Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 2–238（237 aa） Fragment：UNP P19491 residues 25-847 and UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Chain B 2–238（237 aa） Fragment：UNP P19491 residues 25-847 and UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Chain C 2–238（237 aa） Fragment：UNP P19491 residues 25-847 and UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Chain D 2–238（237 aa） Fragment：UNP P19491 residues 25-847 and UNP D3Z7H4 residues 2-238 linked via LINKER GTG
Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.10 Å
5WEN GluA2 bound to GSG1L in digitonin, state 2 Deposited 2017-07-10 Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 2–238（237 aa） Fragment：UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG,UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG
Chain B 2–238（237 aa） Fragment：UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG,UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG
Chain C 2–238（237 aa） Fragment：UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG,UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG
Chain D 2–238（237 aa） Fragment：UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG,UNP residues 25-847 and UNP residues 2-238 linked via LINKER GTG
Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L,N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L,N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L,N241E, V382L, G384E, N385D, N392Q, V1151L Mutation：N241E, V382L, G384E, N385D, N392Q, V1151L,N241E, V382L, G384E, N385D, N392Q, V1151L AJP Digitonin × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 6.80 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.