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Open data
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Basic information
Entry | Database: PDB / ID: 1yfc | ||||||
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Title | Solution nmr structure of a yeast iso-1-ferrocytochrome C | ||||||
![]() | YEAST ISO-1-FERROCYTOCHROME C | ||||||
![]() | ELECTRON TRANSPORT / FERROCYTOCHROME / MITOCHONDRION / RESPIRATORY CHAIN / METHYLATION | ||||||
Function / homology | ![]() Release of apoptotic factors from the mitochondria / Pyroptosis / Detoxification of Reactive Oxygen Species / Respiratory electron transport / cardiolipin binding / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial intermembrane space / electron transfer activity / heme binding ...Release of apoptotic factors from the mitochondria / Pyroptosis / Detoxification of Reactive Oxygen Species / Respiratory electron transport / cardiolipin binding / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / mitochondrial intermembrane space / electron transfer activity / heme binding / mitochondrion / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry | ||||||
![]() | Baistrocchi, P. / Banci, L. / Bertini, I. / Turano, P. / Bren, K.L. / Gray, H.B. | ||||||
![]() | ![]() Title: Three-dimensional solution structure of Saccharomyces cerevisiae reduced iso-1-cytochrome c. Authors: Baistrocchi, P. / Banci, L. / Bertini, I. / Turano, P. / Bren, K.L. / Gray, H.B. #1: ![]() Title: Assignment of Proton Resonances, Identification of Secondary Structural Elements, and Analysis of Backbone Chemical Shifts for the C102T Variant of Yeast Iso-1-Cytochrome C and Horse Cytochrome C Authors: Gao, Y. / Boyd, J. / Williams, R.J. / Pielak, G.J. #2: ![]() Title: High-Resolution Refinement of Yeast Iso-1-Cytochrome C and Comparisons with Other Eukaryotic Cytochromes C Authors: Louie, G.V. / Brayer, G.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 695.6 KB | Display | ![]() |
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PDB format | ![]() | 597.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 12099.850 Da / Num. of mol.: 1 / Mutation: C102S Source method: isolated from a genetically manipulated source Details: REDUCED FORM Source: (gene. exp.) ![]() ![]() Gene: YEAST ISO-1-CYTOCHROME C / Variant: C102S / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-HEC / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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Sample preparation
Sample conditions | pH: 7 / Temperature: 303 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker AMX 600 / Manufacturer: Bruker / Model: AMX 600 / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: distance geometry / Software ordinal: 1 | ||||||
NMR ensemble | Conformer selection criteria: TARGET FUNCTION <= 0.82 A2 / Conformers calculated total number: 500 / Conformers submitted total number: 20 |