Current Protein Identity:P21873 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
1W85 The crystal structure of pyruvate dehydrogenase E1 bound to the peripheral subunit binding domain of E2 Deposited 2004-09-16 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain A 1–368(368 aa)
Chain C 1–368(368 aa)
Not recorded MG MAGNESIUM ION × 3 PEG DI(HYDROXYETHYL)ETHER × 2 TPP THIAMINE DIPHOSPHATE × 2 K POTASSIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5;293 K;10% PEG 5500 MONOMETHYL ETHER, 0.2M IMIDAZOLE MALATE PH5. 20DEG C, SITTING-DROP., pH 5.00
Resolution 2.00 Å R-free 0.215
1W85 The crystal structure of pyruvate dehydrogenase E1 bound to the peripheral subunit binding domain of E2 Deposited 2004-09-16 Assembly 2 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain E 1–368(368 aa)
Chain G 1–368(368 aa)
Not recorded MG MAGNESIUM ION × 3 PEG DI(HYDROXYETHYL)ETHER × 1 TPP THIAMINE DIPHOSPHATE × 2 K POTASSIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5;293 K;10% PEG 5500 MONOMETHYL ETHER, 0.2M IMIDAZOLE MALATE PH5. 20DEG C, SITTING-DROP., pH 5.00
Resolution 2.00 Å R-free 0.215
1W88 The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit binding domain of E2 Deposited 2004-09-16 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain A 1–368(368 aa)
Chain C 1–368(368 aa)
Mutation:YES Mutation:YES MG MAGNESIUM ION × 2 TPP THIAMINE DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5;15% PEG 4000, 0.2M IMIDAZOLE MALATE PH5, pH 5.00
Resolution 2.30 Å R-free 0.262
1W88 The crystal structure of pyruvate dehydrogenase E1(D180N,E183Q) bound to the peripheral subunit binding domain of E2 Deposited 2004-09-16 Assembly 2 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain E 1–368(368 aa)
Chain G 1–368(368 aa)
Mutation:YES Mutation:YES MG MAGNESIUM ION × 2 TPP THIAMINE DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5;15% PEG 4000, 0.2M IMIDAZOLE MALATE PH5, pH 5.00
Resolution 2.30 Å R-free 0.262
3DUF Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex Deposited 2008-07-17 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain A 1–369(369 aa)
Chain C 1–369(369 aa)
Not recorded MG MAGNESIUM ION × 3 R1T 2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-[(1R)-1-HYDROXYETHYL]-3-METHYL-2-THIENYL}ETHYL TRIHYDROGEN DIPHOSPHATE × 2 K POTASSIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;The protein solution was then mixed in 1:1 volume ratio of crystallization buffer consisting of 8-12 % mono-methyl ether polyethylene glycol (MME PEG) 5000, 0.1 M Na maleate pH 5.5, and the droplet was left to equilibrate against a reservoir of neat crystallization buffer., VAPOR DIFFUSION, SITTING DROP, temperature 291.15K
Resolution 2.50 Å R-free 0.263
3DUF Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex Deposited 2008-07-17 Assembly 2 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain E 1–369(369 aa)
Chain G 1–369(369 aa)
Not recorded MG MAGNESIUM ION × 2 R1T 2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-5-[(1R)-1-HYDROXYETHYL]-3-METHYL-2-THIENYL}ETHYL TRIHYDROGEN DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;The protein solution was then mixed in 1:1 volume ratio of crystallization buffer consisting of 8-12 % mono-methyl ether polyethylene glycol (MME PEG) 5000, 0.1 M Na maleate pH 5.5, and the droplet was left to equilibrate against a reservoir of neat crystallization buffer., VAPOR DIFFUSION, SITTING DROP, temperature 291.15K
Resolution 2.50 Å R-free 0.263
3DV0 Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex Deposited 2008-07-18 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain A 1–369(369 aa)
Chain C 1–369(369 aa)
Not recorded MG MAGNESIUM ION × 3 TPW 2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-3-METHYLTHIOPHEN-2-YL}ETHYL TRIHYDROGEN DIPHOSPHATE × 2 K POTASSIUM ION × 2 PYR PYRUVIC ACID × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;10-15% PEG 4K, 0.2 M imidazole malate pH 5 in the presence of 5 mM 3-deazaThDP. The crystals were soaked with 10mM pyruvate for 3-day, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291.15K
Resolution 2.50 Å R-free 0.241
3DV0 Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex Deposited 2008-07-18 Assembly 2 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain E 1–369(369 aa)
Chain G 1–369(369 aa)
Not recorded MG MAGNESIUM ION × 3 TPW 2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-3-METHYLTHIOPHEN-2-YL}ETHYL TRIHYDROGEN DIPHOSPHATE × 2 K POTASSIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;10-15% PEG 4K, 0.2 M imidazole malate pH 5 in the presence of 5 mM 3-deazaThDP. The crystals were soaked with 10mM pyruvate for 3-day, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291.15K
Resolution 2.50 Å R-free 0.241
3DVA Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex Deposited 2008-07-18 Assembly 1 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain A 1–369(369 aa)
Chain C 1–369(369 aa)
Mutation:I206A Mutation:I206A MG MAGNESIUM ION × 3 TPW 2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-3-METHYLTHIOPHEN-2-YL}ETHYL TRIHYDROGEN DIPHOSPHATE × 2 K POTASSIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;The mutant crystals are obtained from sitting-drop vapour diffusion using following condition: 10-15% PEG 4K, 0.2 M imidazole malate pH 5 in the presence of 5 mM 3-deazaThDP, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291.15K
Resolution 2.35 Å R-free 0.247
3DVA Snapshots of catalysis in the E1 subunit of the pyruvate dehydrogenase multi-enzyme complex Deposited 2008-07-18 Assembly 2 Protein heterocomplex Heteromer;Protein × 5 PDB declaration: pentameric(5) Consistent with protein count
Chain E 1–369(369 aa)
Chain G 1–369(369 aa)
Mutation:I206A Mutation:I206A MG MAGNESIUM ION × 3 TPW 2-{4-[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)METHYL]-3-METHYLTHIOPHEN-2-YL}ETHYL TRIHYDROGEN DIPHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;pH 5.5;291.15 K;The mutant crystals are obtained from sitting-drop vapour diffusion using following condition: 10-15% PEG 4K, 0.2 M imidazole malate pH 5 in the presence of 5 mM 3-deazaThDP, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291.15K
Resolution 2.35 Å R-free 0.247