+Open data
-Basic information
Entry | Database: PDB / ID: 1jex | ||||||
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Title | SOLUTION STRUCTURE OF A67V MUTANT OF RAT FERRO CYTOCHROME B5 | ||||||
Components | CYTOCHROME B5 | ||||||
Keywords | ELECTRON TRANSPORT / CYTOCHROME B5 / SOLUTION STRUCTURES | ||||||
Function / homology | Function and homology information Vitamin C (ascorbate) metabolism / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / response to cadmium ion / mitochondrial outer membrane / electron transfer activity / intracellular membrane-bounded organelle / heme binding / endoplasmic reticulum membrane / enzyme binding / endoplasmic reticulum ...Vitamin C (ascorbate) metabolism / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / response to cadmium ion / mitochondrial outer membrane / electron transfer activity / intracellular membrane-bounded organelle / heme binding / endoplasmic reticulum membrane / enzyme binding / endoplasmic reticulum / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | Rattus norvegicus (Norway rat) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Shahzad, N. / Dangi, B. / Blankman, J.I. / Guiles, R.D. | ||||||
Citation | Journal: To be Published Title: MUTAGENIC MODULATION OF THE ENTROPY CHANGE ON OXIDATION OF CYTOCHROME B5: AN ANALYSIS OF THE CONTRIBUTION OF CONFORMATIONAL ENTROPY Authors: SHAHZAD, N. / DANGI, B. / BLANKMAN, J.I. / GUILES, R.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1jex.cif.gz | 561.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1jex.ent.gz | 487.1 KB | Display | PDB format |
PDBx/mmJSON format | 1jex.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/je/1jex ftp://data.pdbj.org/pub/pdb/validation_reports/je/1jex | HTTPS FTP |
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-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: 10841.962 Da / Num. of mol.: 1 / Mutation: A67V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: PET3C / Production host: Escherichia coli (E. coli) / References: UniProt: P00173 |
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#2: Chemical | ChemComp-HEM / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 2MM F35Y CYTOCHROME B5;1MM PHOSPHATE BUFFER; PURGED WITH NITROGEN GAS AND REDUCED BY ADDING FEW GRAINS OF SODIUM DITHIONATE AND SEALED USING OXY-ACETYLENE TORCH; 0.05 MM TSP AS INTERNAL REFERENCE Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 1 mM / pH: 7.0 / Pressure: ambient / Temperature: 313 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: THE STRUCTURE WAS CALCULATED USING 1177 NOE RESTRAINTS AND 75 DIHEDRAL ANGLE RESTRAINTS; RESIDUES 1-3 AND 89-94 WERE NOT INCLUDED IN THE REFINED MODEL BECAUSE OF A LACK OF RESTRAINTS IN ...Details: THE STRUCTURE WAS CALCULATED USING 1177 NOE RESTRAINTS AND 75 DIHEDRAL ANGLE RESTRAINTS; RESIDUES 1-3 AND 89-94 WERE NOT INCLUDED IN THE REFINED MODEL BECAUSE OF A LACK OF RESTRAINTS IN THESE PRESUMABLY UNSTRUCTURED REGIONS OF THE PROTEIN. | ||||||||||||||||||||
NMR representative | Selection criteria: fewest violations, lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry, structures with the least restraint violations, target function Conformers calculated total number: 200 / Conformers submitted total number: 20 |