Current Protein Identity:P39099 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state 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
3STI Crystal structure of the protease domain of DegQ from Escherichia coli Deposited 2011-07-11 Assembly 1 Protein homooligomer Homooligomer;Protein × 3 PDB declaration: trimeric(3) Consistent with protein count
Chain A 28–264(237 aa) Fragment:UNP residues 28-264
Chain B 28–264(237 aa) Fragment:UNP residues 28-264
Chain C 28–264(237 aa) Fragment:UNP residues 28-264
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 7;291 K;1.6M Ammonium sulfate, 3% PEG 400, 0.1M Hepes, pH7.0 , VAPOR DIFFUSION, temperature 291K
Resolution 2.60 Å R-free 0.257
3STJ Crystal structure of the protease + PDZ1 domain of DegQ from Escherichia coli Deposited 2011-07-11 Assembly 1 Protein heterocomplex Heteromer;Protein × 7 PDB declaration: heptameric(7) Consistent with protein count
Chain A 28–364(337 aa) Fragment:UNP residues 28-364
Chain B 28–364(337 aa) Fragment:UNP residues 28-364
Chain C 28–364(337 aa) Fragment:UNP residues 28-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 5.4;291 K;24% PEG6000, 5% PEG100, 10% glycerol, 0.1M MES pH5.4, VAPOR DIFFUSION, temperature 291K
Resolution 2.60 Å R-free 0.212
3STJ Crystal structure of the protease + PDZ1 domain of DegQ from Escherichia coli Deposited 2011-07-11 Assembly 2 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric(6) Consistent with protein count
Chain D 28–364(337 aa) Fragment:UNP residues 28-364
Chain E 28–364(337 aa) Fragment:UNP residues 28-364
Chain F 28–364(337 aa) Fragment:UNP residues 28-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 5.4;291 K;24% PEG6000, 5% PEG100, 10% glycerol, 0.1M MES pH5.4, VAPOR DIFFUSION, temperature 291K
Resolution 2.60 Å R-free 0.212
3STJ Crystal structure of the protease + PDZ1 domain of DegQ from Escherichia coli Deposited 2011-07-11 Assembly 3 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric(6) Consistent with protein count
Chain G 28–364(337 aa) Fragment:UNP residues 28-364
Chain H 28–364(337 aa) Fragment:UNP residues 28-364
Chain I 28–364(337 aa) Fragment:UNP residues 28-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 5.4;291 K;24% PEG6000, 5% PEG100, 10% glycerol, 0.1M MES pH5.4, VAPOR DIFFUSION, temperature 291K
Resolution 2.60 Å R-free 0.212
3STJ Crystal structure of the protease + PDZ1 domain of DegQ from Escherichia coli Deposited 2011-07-11 Assembly 4 Protein heterocomplex Heteromer;Protein × 6 PDB declaration: hexameric(6) Consistent with protein count
Chain J 28–364(337 aa) Fragment:UNP residues 28-364
Chain K 28–364(337 aa) Fragment:UNP residues 28-364
Chain L 28–364(337 aa) Fragment:UNP residues 28-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 5.4;291 K;24% PEG6000, 5% PEG100, 10% glycerol, 0.1M MES pH5.4, VAPOR DIFFUSION, temperature 291K
Resolution 2.60 Å R-free 0.212
3STJ Crystal structure of the protease + PDZ1 domain of DegQ from Escherichia coli Deposited 2011-07-11 Assembly 5 Protein heterocomplex Heteromer;Protein × 25 PDB declaration: 25-meric(25) Consistent with protein count
Chain A 28–364(337 aa) Fragment:UNP residues 28-364
Chain B 28–364(337 aa) Fragment:UNP residues 28-364
Chain C 28–364(337 aa) Fragment:UNP residues 28-364
Chain D 28–364(337 aa) Fragment:UNP residues 28-364
Chain E 28–364(337 aa) Fragment:UNP residues 28-364
Chain F 28–364(337 aa) Fragment:UNP residues 28-364
Chain G 28–364(337 aa) Fragment:UNP residues 28-364
Chain H 28–364(337 aa) Fragment:UNP residues 28-364
Chain I 28–364(337 aa) Fragment:UNP residues 28-364
Chain J 28–364(337 aa) Fragment:UNP residues 28-364
Chain K 28–364(337 aa) Fragment:UNP residues 28-364
Chain L 28–364(337 aa) Fragment:UNP residues 28-364
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 5.4;291 K;24% PEG6000, 5% PEG100, 10% glycerol, 0.1M MES pH5.4, VAPOR DIFFUSION, temperature 291K
Resolution 2.60 Å R-free 0.212
4A8A Asymmetric cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozyme Deposited 2011-11-20 Assembly 1 Protein heterocomplex Heteromer;Protein × 13 PDB declaration: tridecameric(13) Consistent with protein count
Chain A 28–455(428 aa)
Chain B 28–455(428 aa)
Chain C 28–455(428 aa)
Chain D 28–455(428 aa)
Chain E 28–455(428 aa)
Chain F 28–455(428 aa)
Chain G 28–455(428 aa)
Chain H 28–455(428 aa)
Chain I 28–455(428 aa)
Chain J 28–455(428 aa)
Chain K 28–455(428 aa)
Chain L 28–455(428 aa)
Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM HEPES/NAOH, 150 MM NACL;pH 7.5;20 MM HEPES/NAOH, 150 MM NACL
cryo-EM vitrification conditions Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, INSTRUMENT- MANUAL PLUNGER, METHOD- BLOT FOR 2 SECONDS BEFORE PLUNGING,
Resolution 14.20 Å
4A8B Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with lysozymes Deposited 2011-11-20 Assembly 1 Protein heterocomplex Heteromer;Protein × 18 PDB declaration: octadecameric(18) Consistent with protein count
Chain A 28–455(428 aa)
Chain B 28–455(428 aa)
Chain C 28–455(428 aa)
Chain D 28–455(428 aa)
Chain E 28–455(428 aa)
Chain F 28–455(428 aa)
Chain G 28–455(428 aa)
Chain H 28–455(428 aa)
Chain I 28–455(428 aa)
Chain J 28–455(428 aa)
Chain K 28–455(428 aa)
Chain L 28–455(428 aa)
Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM HEPES/NAOH, 150 MM NACL;pH 7.5;20 MM HEPES/NAOH, 150 MM NACL
cryo-EM vitrification conditions Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, INSTRUMENT- MANUAL PLUNGER, METHOD- BLOT FOR 2 SECONDS BEFORE PLUNGING,
Resolution 13.00 Å
4A8C Symmetrized cryo-EM reconstruction of E. coli DegQ 12-mer in complex with a binding peptide Deposited 2011-11-20 Assembly 1 Protein homooligomer Homooligomer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count
Chain A 28–455(428 aa)
Chain B 28–455(428 aa)
Chain C 28–455(428 aa)
Chain D 28–455(428 aa)
Chain E 28–455(428 aa)
Chain F 28–455(428 aa)
Chain G 28–455(428 aa)
Chain H 28–455(428 aa)
Chain I 28–455(428 aa)
Chain J 28–455(428 aa)
Chain K 28–455(428 aa)
Chain L 28–455(428 aa)
Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 20 MM HEPES/NAOH, 150 MM NACL;pH 7.5;20 MM HEPES/NAOH, 150 MM NACL
cryo-EM vitrification conditions Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, INSTRUMENT- MANUAL PLUNGER, METHOD- BLOT FOR 2 SECONDS BEFORE PLUNGING,
Resolution 7.50 Å
4A9G Symmetrized cryo-EM reconstruction of E. coli DegQ 24-mer in complex with beta-casein Deposited 2011-11-26 Assembly 1 Protein homooligomer Homooligomer;Protein × 24 PDB declaration: 24-meric(24) Consistent with protein count
Chain A 28–455(428 aa)
Chain B 28–455(428 aa)
Chain C 28–455(428 aa)
Chain D 28–455(428 aa)
Chain E 28–455(428 aa)
Chain F 28–455(428 aa)
Chain G 28–455(428 aa)
Chain H 28–455(428 aa)
Chain I 28–455(428 aa)
Chain J 28–455(428 aa)
Chain K 28–455(428 aa)
Chain L 28–455(428 aa)
Chain M 28–455(428 aa)
Chain N 28–455(428 aa)
Chain O 28–455(428 aa)
Chain P 28–455(428 aa)
Chain Q 28–455(428 aa)
Chain R 28–455(428 aa)
Chain S 28–455(428 aa)
Chain T 28–455(428 aa)
Chain U 28–455(428 aa)
Chain V 28–455(428 aa)
Chain W 28–455(428 aa)
Chain Y 28–455(428 aa)
Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES Mutation:YES No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer 150MM NACL, 20MM HEPES/NAOH;pH 7.5;150MM NACL, 20MM HEPES/NAOH
cryo-EM vitrification conditions Cryogen ETHANE;LIQUID ETHANE
Resolution 7.50 Å