Current Protein Identity:Q5QNQ1
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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 |
|---|---|---|---|---|---|---|---|
| 9M0X Cryo-EM structure of the agmatine-bound zTAAR13d-Gs complex Deposited 2025-02-25 | Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count |
Chain R
1–341(341 aa)
|
Not recorded | AG2 AGMATINE × 2 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.71 Å |
| 9M0Z Cryo-EM structure of the cadaverine-bound zTAAR13d-Gs complex Deposited 2025-02-25 | Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count |
Chain R
1–341(341 aa)
|
Not recorded | N2P PENTANE-1,5-DIAMINE × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.74 Å |
| 9M1P Cryo-EM structure of the histamine-bound zTAAR13d-Gs complex Deposited 2025-02-26 | Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count |
Chain R
1–341(341 aa)
|
Not recorded | HSM HISTAMINE × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.80 Å |
| 9M2O Cryo-EM structure of the putrescine-bound zTAAR13d-Gs complex Deposited 2025-02-28 | Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count |
Chain R
1–341(341 aa)
|
Not recorded | PUT 1,4-DIAMINOBUTANE × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE
|
Resolution 2.59 Å |