Current Protein Identity:Q91MK1 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification 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
4KYC Structure of the C-terminal domain of the Menangle virus phosphoprotein, fused to MBP. Deposited 2013-05-28 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 339–388(50 aa) Fragment:unprot P0AEX9 residues 27-392, unprot Q91MK1 residues 339-388
Mutation:E172A, N173A, E359A, K362A, D363A, C352S EDO 1,2-ETHANEDIOL × 1 BO3 BORIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 9.1;291.15 K;24 %(w/v) PEG8000, 0.2 M Boric acid/KOH, pH 9.1, VAPOR DIFFUSION, SITTING DROP, temperature 291.15K
Resolution 1.95 Å R-free 0.213
7KD4 Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P21. Deposited 2020-10-08 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 329–388(60 aa)
Mutation:C352S SO4 SULFATE ION × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, Crystals were transferred into the following cryo-protective solution before vitrification: 1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, 5mM Maltose, 1 M Lithium sulfate
Resolution 1.31 Å R-free 0.196
7KD4 Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P21. Deposited 2020-10-08 Assembly 2 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 329–388(60 aa)
Mutation:C352S SO4 SULFATE ION × 7 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, Crystals were transferred into the following cryo-protective solution before vitrification: 1.65 M Ammonium sulphate, 0.2M Malic acid/KOH pH 5.5, 5mM Maltose, 1 M Lithium sulfate
Resolution 1.31 Å R-free 0.196
7KD5 Structure of the C-terminal domain of the Menangle virus phosphoprotein (residues 329 -388), fused to MBP. Space group P212121 Deposited 2020-10-08 Assembly 1 Insufficient information Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 329–388(60 aa)
Mutation:C352S EDO 1,2-ETHANEDIOL × 4 PIN PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID) × 3 PRO PROLINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 6.7;291.15 K;20%(w/v) PEG 5000 mono-methyl ether, 0.2 M Pipes/KOH pH 6.7, 0.1M Proline, Crystals were transferred into the following cryo-protective solution before vitrification: 20%(w/v) PEG 5000 mono-methyl ether, 0.2 M Pipes/KOH pH 6.7, 0.1M Proline, 5mM Maltose, 20%(v/v) Ethylene Glycol
Resolution 1.55 Å R-free 0.189