|Entry||Database: PDB / ID: 2orl|
|Title||Solution structure of the cytochrome c- para-aminophenol adduct|
|Components||Cytochrome c iso-1|
|Keywords||ELECTRON TRANSPORT / protein-ligand adduct|
|Function / homology|
Function and homology information
Detoxification of Reactive Oxygen Species / Respiratory electron transport / Release of apoptotic factors from the mitochondria / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / respirasome / mitochondrial intermembrane space / electron transfer activity / heme binding / mitochondrion / metal ion binding
Cytochrome c, class IA/ IB / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Cytochrome c / Cytochrome c family profile.
Cytochrome c iso-1
|Biological species||Saccharomyces cerevisiae (baker's yeast)|
|Method||SOLUTION NMR / combined docking, simulated annealing with NMR restraints|
|Authors||Assfalg, M. / Bertini, I. / Del Conte, R. / Giachetti, A. / Turano, P.|
|Citation||Journal: Biochemistry / Year: 2007|
Title: Cytochrome c and organic molecules: solution structure of the p-aminophenol adduct.
Authors: Assfalg, M. / Bertini, I. / Del Conte, R. / Giachetti, A. / Turano, P.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
A: Cytochrome c iso-1
|#1: Protein/peptide|| |
Mass: 12071.796 Da / Num. of mol.: 1 / Mutation: C102T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (baker's yeast)
Gene: CYC1 / Production host: Escherichia coli (E. coli) / References: UniProt: P00044
|#2: Chemical|| ChemComp-HEC / |
|#3: Chemical|| ChemComp-4NL / |
|Experiment||Method: SOLUTION NMR|
|NMR experiment||Type: 3D 15N-separated NOESY|
|Details||Contents: 2-3mM Cytochrome c U-15N, 50mM phosphate buffer, pH 7.0, 90% H2O, 10% D2O|
Solvent system: 90% H2O/10% D2O
|Sample conditions||Ionic strength: 50 mM phosphate buffer / pH: 7.0 / Pressure: 1 atm / Temperature: 303 K|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M|
|Radiation wavelength||Relative weight: 1|
|NMR spectrometer||Type: Bruker Avance / Manufacturer: Bruker / Model: Avance / Field strength: 800 MHz|
|Refinement||Method: combined docking, simulated annealing with NMR restraints|
Software ordinal: 1
Details: four intermolecular NOEs were used together with intra-protein NOEs and angle constraints
|NMR representative||Selection criteria: lowest energy|
|NMR ensemble||Conformer selection criteria: structure with the lowest interaction energy|
Conformers calculated total number: 100 / Conformers submitted total number: 25
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