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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：Q99969 New Search
11PDB entries
11Biological assembly
11chain/assembly records
Main Difference Dimensions in This Set
Different construct 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
7YKD Cryo-EM structure of the human chemerin receptor 1 complex with the C-terminal nonapeptide of chemerin Deposited 2022-07-22 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain L 149–157（9 aa）
Not recorded CLR CHOLESTEROL × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.81 Å
8JJP G protein-coupled receptor 1 Deposited 2023-05-31 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain L 149–157（9 aa）
Not recorded CLR CHOLESTEROL × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
8XGM Cryo-EM structure of human GPR1 bound to chemerin Deposited 2023-12-15 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain D 21–157（137 aa）
Not recorded CLR CHOLESTEROL × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.29 Å
8ZJG Cryo-EM structure of human CMKLR1-Gi complex bound to chemerin Deposited 2024-05-14 Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain L 21–157（137 aa）
Not recorded CLR CHOLESTEROL × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.18 Å
9L3W Cryo-EM structure of the chemokine-like receptor 1 in complex with chemerin and Gi1 Deposited 2024-12-19 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain L 21–157（137 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
9L3Y Cryo-EM structure of the G-protein coupled receptor 1 (GPR1) in complex with chemerin and Gi1 Deposited 2024-12-19 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain L 21–157（137 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.60 Å
9UYH Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 1) Deposited 2025-05-15 Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain L 20–157（138 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9UYI Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 2) Deposited 2025-05-15 Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain L 20–157（138 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
9UYJ Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 3) Deposited 2025-05-15 Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain L 20–157（138 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9UYL Cryo-EM structure of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 1 (Conformation 4) Deposited 2025-05-15 Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain L 20–157（138 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
9UYM Composite map of the G protein-coupled receptor 1 (GPR1) bound to chemerin and beta-arrestin 2 Deposited 2025-05-15 Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain L 20–157（138 aa）
Not recorded Y01 CHOLESTEROL HEMISUCCINATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 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.