← Back to search

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：Q53687 New Search
2PDB entries
3Biological assembly
16chain/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
7TEA Crystal structure of S. aureus GlnR-DNA complex Deposited 2022-01-04 Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric（4） Consistent with all polymers
Chain B 1–83（83 aa）
Chain E 1–83（83 aa）
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；275 K；50 mM sodium cacodylate pH 6.5, 13% PEG 8000, 0.15 M calcium acetate, 20% glycerol
Resolution 2.35 Å R-free 0.264
7TEA Crystal structure of S. aureus GlnR-DNA complex Deposited 2022-01-04 Assembly 2 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric（4） Consistent with all polymers
Chain A 1–83（83 aa）
Chain C 1–83（83 aa）
Not recorded CA CALCIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；275 K；50 mM sodium cacodylate pH 6.5, 13% PEG 8000, 0.15 M calcium acetate, 20% glycerol
Resolution 2.35 Å R-free 0.264
7TF6 S. aureus GS(12)-Q-GlnR peptide Deposited 2022-01-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 24 PDB declaration: 24-meric（24） Consistent with protein count
Chain D 111–121（11 aa） Fragment：Residues 111-121
Chain E 111–121（11 aa） Fragment：Residues 111-121
Chain I 111–121（11 aa） Fragment：Residues 111-121
Chain J 111–121（11 aa） Fragment：Residues 111-121
Chain K 111–121（11 aa） Fragment：Residues 111-121
Chain M 111–121（11 aa） Fragment：Residues 111-121
Chain P 111–121（11 aa） Fragment：Residues 111-121
Chain Q 111–121（11 aa） Fragment：Residues 111-121
Chain U 111–121（11 aa） Fragment：Residues 111-121
Chain V 111–121（11 aa） Fragment：Residues 111-121
Chain W 111–121（11 aa） Fragment：Residues 111-121
Chain X 111–121（11 aa） Fragment：Residues 111-121
Not recorded MG MAGNESIUM ION × 24 GLN GLUTAMINE × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.15 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.