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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：Q8WWW0 New Search
2PDB entries
7Biological assembly
9chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion 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
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain E 365–413（49 aa） Fragment：SARAH domain, UNP residues 365-413
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27 Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain G 365–413（49 aa） Fragment：SARAH domain, UNP residues 365-413
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 1 NA SODIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27 Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain H 365–413（49 aa） Fragment：SARAH domain, UNP residues 365-413
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 3 NA SODIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27 Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain F 365–413（49 aa） Fragment：SARAH domain, UNP residues 365-413
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 1 MG MAGNESIUM ION × 1 SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27 Assembly 5 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain E 365–413（49 aa） Fragment：SARAH domain, UNP residues 365-413
Chain F 365–413（49 aa） Fragment：SARAH domain, UNP residues 365-413
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.05 Å R-free 0.244
4LGD Structural Basis for Autoactivation of Human Mst2 Kinase and Its Regulation by RASSF5 Deposited 2013-06-27 Assembly 6 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain G 365–413（49 aa） Fragment：SARAH domain, UNP residues 365-413
Chain H 365–413（49 aa） Fragment：SARAH domain, UNP residues 365-413
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 SO4 SULFATE ION × 4 NA SODIUM ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；293 K；0.1 M Bis-Tris propane, 200 mM Na2SO4, 20% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 3.05 Å R-free 0.244
4OH8 Crystal Structure of the human MST1-RASSF5 SARAH heterodimer Deposited 2014-01-17 Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain B 366–418（53 aa） Fragment：RASSF5 SARAH domain
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 4.8；293 K；35% (v/v) 2-methyl-2,4-pentanediol (MPD) acetate, pH 4.8, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.28 Å R-free 0.278

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.