Current Protein Identity:P82599 New Search
Main Difference Dimensions in This Set
Different mutation/modification 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
1B7V Structure of the C-553 cytochrome from Bacillus pasteruii to 1.7 A resolution Deposited 1999-01-22 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 22–92(71 aa)
Not recorded HEC HEME C × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;8MG/ML OF CYTOCHROME, 20MM TRIS.HCL, PH 8.0 AT 20 DEGREES C, HANGING DROPS IN HAMPTON RESEARCH 24-WELL LINBRO PLATES, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.70 Å R-free 0.206
1C75 0.97 A "AB INITIO" CRYSTAL STRUCTURE OF CYTOCHROME C-553 FROM BACILLUS PASTEURII Deposited 2000-02-09 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 22–92(71 aa)
Not recorded HEC HEME C × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5;3.2 M AMMONIUM SULPHATE IN 100 MM SODIUM CITRATE BUFFER PH 5.0
Resolution 0.97 Å
1K3G NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii Deposited 2001-10-03 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 22–92(71 aa) Fragment:residues 22-92
Not recorded HEC HEME C × 1 SOLUTION NMR
NMR measurement conditions pH 7.5;288 K;Ionic strength (raw mmCIF value) 10 mM phosphate buffer;Pressure Ambient
NMR sample composition 1-3 mM oxidized cytochrome c-553 in 10 mM phosphate buffer | 90%H2O+10%D2O; 100% D2O
Resolution not provided
1K3H NMR Solution Structure of Oxidized Cytochrome c-553 from Bacillus pasteurii Deposited 2001-10-03 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 22–92(71 aa) Fragment:RESIDUES 22-92
Not recorded HEC HEME C × 1 SOLUTION NMR
NMR measurement conditions pH 7.5;288 K;Ionic strength (raw mmCIF value) 10 mM phosphate buffer;Pressure Ambient
NMR sample composition 1-3 mM oxidized cytochrome c-553 in 10 mM phosphate buffer | 90%H2O+10%D2O; 100% D2O
Resolution not provided
1N9C Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processes Deposited 2002-11-23 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 22–92(71 aa) Fragment:soluble part of membrane-anchored cytochrome c
Not recorded HEC HEME C × 1 SOLUTION NMR
NMR measurement conditions pH 7;296 K;Ionic strength (raw mmCIF value) 100 mM Pi;Pressure ambient
NMR sample composition 2 mM cytochrome, 100mM phosphate buffer, pH 7.0 | 90% H2O/10% D2O
NMR sample composition 1 mM cytochrome U-15N, 100mM phosphate buffer, pH 7.0 | 90% H2O/10% D2O
Resolution not provided