Current Protein Identity:P39099
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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 |