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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：A0A2R4KP93 New Search
5PDB entries
5Biological assembly
11chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
8SAK BtCoV-422 in complex with neutralizing antibody JC57-11 Deposited 2023-04-01 Assembly 1 Other combination Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain A 1–1289（1289 aa）
Chain B 1–1289（1289 aa）
Chain C 1–1289（1289 aa）
Mutation：A885P, A1056P, V1057P Mutation：A885P, A1056P, V1057P Mutation：A885P, A1056P, V1057P NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 18 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
9JMJ Cryo-EM structure of the GD-BatCoV (BtCoV/Ii/GD/2014-422) RBD in complex with human DPP4 Deposited 2024-09-20 Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 371–610（240 aa） Fragment：RBD,RBD
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9JMP Cryo-EM structure of GD-BatCoV (BtCoV/Ii/GD/2014-422) S-trimer Deposited 2024-09-20 Assembly 1 Insufficient information Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–1294（1294 aa）
Chain B 1–1294（1294 aa）
Chain C 1–1294（1294 aa）
Mutation：A885P,S962P,A969P,N1012P,A1056P,V1057P Mutation：A885P,S962P,A969P,N1012P,A1056P,V1057P Mutation：A885P,S962P,A969P,N1012P,A1056P,V1057P NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 EIC LINOLEIC ACID × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
9UEB Prefusion structure of 2014-422 spike glycoprotein Deposited 2025-04-08 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 1–1288（1288 aa）
Chain B 1–1288（1288 aa）
Chain C 1–1288（1288 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 26 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.59 Å
9V2L Complex structure of 2014-422 spike RBD bound to human DPP4 Deposited 2025-05-20 Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 371–593（223 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 7 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 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.