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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：P33032 New Search
3PDB entries
3Biological assembly
3chain/assembly records
Main Difference Dimensions in This Set
Different construct Different assembly state 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
8INR Cryo-EM structure of the alpha-MSH-bound human melanocortin receptor 5 (MC5R)-Gs complex Deposited 2023-03-10 Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain R 2–325（324 aa）
Not recorded CA CALCIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.73 Å
8IOD Cryo-EM structure of the PG-901-bound human melanocortin receptor 5 (MC5R)-Gs complex Deposited 2023-03-10 Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric（6） Consistent with protein count
Chain R 2–325（324 aa）
Not recorded CA CALCIUM ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.59 Å
9K3H Cryo-EM structure of the unliganded human melanocortin receptor 5 (MC5R)-Gs complex Deposited 2024-10-18 Assembly 1 Insufficient information Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain R 1–325（325 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.86 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.