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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：P32495 New Search
4PDB entries
4Biological assembly
6chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method 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
2LBW Solution structure of the S. cerevisiae H/ACA RNP protein Nhp2p-S82W mutant Deposited 2011-04-07 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 36–156（121 aa） Fragment：SEQUENCE DATABASE RESIDUES 36-156
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.2；Pressure ambient
NMR sample composition 20 mM [U-13C; U-15N] HEPES, 200 mM [U-13C; U-15N] potassium chloride, 1 mM [U-13C; U-15N] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 20 mM [U-15N] HEPES, 200 mM [U-15N] potassium chloride, 1 mM [U-15N] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 20 mM [U-13C; U-15N] HEPES, 200 mM [U-13C; U-15N] potassium chloride, 1 mM [U-13C; U-15N] DTT, 100% D2O | 100% D2O
Resolution not provided
2LBX Solution structure of the S. cerevisiae H/ACA RNP protein Nhp2p Deposited 2011-04-07 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 36–156（121 aa） Fragment：sequence database residues 36-156
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.2；Pressure ambient
NMR sample composition 20 mM [U-13C; U-15N] HEPES, 200 mM [U-13C; U-15N] potassium chloride, 1 mM [U-13C; U-15N] DTT, 100% D2O | 100% D2O
NMR sample composition 20 mM [U-15N] HEPES, 200 mM [U-15N] potassium chloride, 1 mM [U-15N] DTT, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 20 mM [U-13C; U-15N] HEPES, 200 mM [U-13C; U-15N] potassium chloride, 1 mM [U-13C; U-15N] DTT, 100% D2O | 100% D2O
Resolution not provided
9G25 snR30 snoRNP - State 1 - Utp23-Krr1-deltaC3 Deposited 2024-07-10 Assembly 1 Protein–RNA Heteromer；Protein × 12 PDB declaration: 14-meric（14） Consistent with all polymers
Chain D 1–156（156 aa）
Chain G 1–156（156 aa）
Not recorded ZN ZINC ION × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.89 Å
9G28 snR30 snoRNP - State 2 - Utp23-Krr1-deltaC3 Deposited 2024-07-10 Assembly 1 Protein–RNA Heteromer；Protein × 12 PDB declaration: 14-meric（14） Consistent with all polymers
Chain D 1–156（156 aa）
Chain G 1–156（156 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.18 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.