Current Protein Identity:A0A1X3JBW6
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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 |
|---|---|---|---|---|---|---|---|
| 8AKN Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the terminating ribosome Deposited 2022-07-30 | Assembly 1 Protein–RNA Heteromer;Protein × 51 PDB declaration: 57-meric(57) Consistent with all polymers |
Chain m
1–127(127 aa)
|
Not recorded | ZN ZINC ION × 2 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1 MG MAGNESIUM ION × 305 SPM SPERMINE × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE
|
Resolution 2.30 Å |
| 8AM9 Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the elongating ribosome Deposited 2022-08-03 | Assembly 1 Protein–RNA Heteromer;Protein × 50 PDB declaration: 56-meric(56) Consistent with all polymers |
Chain m
1–127(127 aa)
|
Not recorded | ZN ZINC ION × 2 MG MAGNESIUM ION × 293 SPM SPERMINE × 1 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE
|
Resolution 2.80 Å |
| 8ANA Cryo-EM structure of the proline-rich antimicrobial peptide drosocin bound to the 50S ribosomal subunit Deposited 2022-08-05 | Assembly 1 Protein–RNA Heteromer;Protein × 30 PDB declaration: 32-meric(32) Consistent with all polymers |
Chain m
1–127(127 aa)
|
Not recorded | ZN ZINC ION × 2 A2G 2-acetamido-2-deoxy-alpha-D-galactopyranose × 1 MG MAGNESIUM ION × 216 SPM SPERMINE × 1 | ELECTRON MICROSCOPY |
cryo-EM buffer
pH 7.4
cryo-EM vitrification conditions
Cryogen ETHANE-PROPANE
|
Resolution 2.10 Å |