Current Protein Identity:A0A5G2R2V2 New Search
Main Difference Dimensions in This Set
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
7NSH 39S mammalian mitochondrial large ribosomal subunit with mtRRF (post) and mtEFG2 Deposited 2021-03-07 Assembly 1 Protein–RNA Heteromer;Protein × 59 PDB declaration: 61-meric(61) Consistent with all polymers
Chain Bd 1–206(206 aa)
Not recorded MG MAGNESIUM ION × 221 ZN ZINC ION × 3 5GP GUANOSINE-5'-MONOPHOSPHATE × 2 SPM SPERMINE × 2 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.20 Å
7NSI 55S mammalian mitochondrial ribosome with mtRRF (pre) and tRNA(P/E) Deposited 2021-03-07 Assembly 1 Protein–RNA Heteromer;Protein × 88 PDB declaration: 93-meric(93) Consistent with all polymers
Chain Bd 1–206(206 aa)
Not recorded MG MAGNESIUM ION × 327 ZN ZINC ION × 6 SPM SPERMINE × 3 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 4.60 Å
7NSJ 55S mammalian mitochondrial ribosome with tRNA(P/P) and tRNA(E*) Deposited 2021-03-07 Assembly 1 Protein–RNA Heteromer;Protein × 87 PDB declaration: 93-meric(93) Consistent with all polymers
Chain Bd 1–206(206 aa)
Not recorded MG MAGNESIUM ION × 324 ZN ZINC ION × 6 SPM SPERMINE × 3 5GP GUANOSINE-5'-MONOPHOSPHATE × 1 GTP GUANOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE-PROPANE
Resolution 3.90 Å