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Yorodumi- PDB-2frc: CYTOCHROME C (REDUCED) FROM EQUUS CABALLUS, NMR, MINIMIZED AVERAG... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2frc | |||||||||
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Title | CYTOCHROME C (REDUCED) FROM EQUUS CABALLUS, NMR, MINIMIZED AVERAGE STRUCTURE | |||||||||
Components | CYTOCHROME C | |||||||||
Keywords | ELECTRON TRANSPORT | |||||||||
Function / homology | Function and homology information cytochrome c-heme linkage / cytochrome complex / positive regulation of cysteine-type endopeptidase activity / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / : / mitochondrial intermembrane space / electron transfer activity / positive regulation of apoptotic process ...cytochrome c-heme linkage / cytochrome complex / positive regulation of cysteine-type endopeptidase activity / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / positive regulation of cysteine-type endopeptidase activity involved in apoptotic process / : / mitochondrial intermembrane space / electron transfer activity / positive regulation of apoptotic process / lipid binding / apoptotic process / heme binding / identical protein binding / metal ion binding / cytosol Similarity search - Function | |||||||||
Biological species | Equus caballus (horse) | |||||||||
Method | SOLUTION NMR / SIMMULATED ANNEALING | |||||||||
Authors | Qi, P.X. / Di Stefano, D.L. / Wand, A.J. | |||||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Solution structure of horse heart ferricytochrome c and detection of redox-related structural changes by high-resolution 1H NMR. Authors: Qi, P.X. / Beckman, R.A. / Wand, A.J. #1: Journal: Nat.Struct.Biol. / Year: 1994 Title: Structural Water in Oxidized and Reduced Horse Heart Cytochrome C Authors: Qi, P.X. / Urbauer, J.L. / Fuentes, E.J. / Leopold, M.F. / Wand, A.J. #2: Journal: Biochemistry / Year: 1994 Title: Solution Structure of Horse Heart Ferrocytochrome C Determined by High-Resolution NMR and Restrained Simulated Annealing Authors: Qi, P.X. / Di Stefano, D.L. / Wand, A.J. #3: Journal: Biochemistry / Year: 1989 Title: Proton Resonance Assignments of Horse Ferrocytochrome C Authors: Wand, A.J. / Di Stefano, D.L. / Feng, Y.Q. / Roder, H. / Englander, S.W. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2frc.cif.gz | 45.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2frc.ent.gz | 36.9 KB | Display | PDB format |
PDBx/mmJSON format | 2frc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2frc_validation.pdf.gz | 452.2 KB | Display | wwPDB validaton report |
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Full document | 2frc_full_validation.pdf.gz | 474.8 KB | Display | |
Data in XML | 2frc_validation.xml.gz | 7.4 KB | Display | |
Data in CIF | 2frc_validation.cif.gz | 9.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fr/2frc ftp://data.pdbj.org/pub/pdb/validation_reports/fr/2frc | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11725.598 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: REDUCED / Source: (natural) Equus caballus (horse) / Organ: HEART / References: UniProt: P00004 |
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#2: Chemical | ChemComp-HEC / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Sample conditions | pH: 5.7 / Temperature: 293 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
Software |
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NMR software |
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Refinement | Method: SIMMULATED ANNEALING / Software ordinal: 1 | |||||||||
NMR ensemble | Conformer selection criteria: LOWEST PENALTY / Conformers calculated total number: 256 / Conformers submitted total number: 1 |