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- PDB-1i8c: SOLUTION STRUCTURE OF THE WATER-SOLUBLE FRAGMENT OF RAT HEPATIC A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1i8c | ||||||
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Title | SOLUTION STRUCTURE OF THE WATER-SOLUBLE FRAGMENT OF RAT HEPATIC APOCYTOCHROME B5 | ||||||
![]() | CYTOCHROME B5 | ||||||
![]() | ELECTRON TRANSPORT / apo hemoprotein | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing, molecular dynamics | ||||||
![]() | Falzone, C.J. / Wang, Y. / Vu, B.C. / Scott, N.L. / Bhattacharya, S. / Lecomte, J.T. | ||||||
![]() | ![]() Title: Structural and dynamic perturbations induced by heme binding in cytochrome b5. Authors: Falzone, C.J. / Wang, Y. / Vu, B.C. / Scott, N.L. / Bhattacharya, S. / Lecomte, J.T. #1: ![]() Title: Design Challenges for Hemoproteins: The Solution Structure of Apocytochrome b5 Authors: Falzone, C.J. / Mayer, M.R. / Whiteman, E.L. / Moore, C.D. / Lecomte, J.T.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 43.6 KB | Display | ![]() |
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PDB format | ![]() | 31.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 244.4 KB | Display | ![]() |
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Full document | ![]() | 244.2 KB | Display | |
Data in XML | ![]() | 3.4 KB | Display | |
Data in CIF | ![]() | 4.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 11229.305 Da / Num. of mol.: 1 / Fragment: WATER-SOLUBLE DOMAIN (RESIDUES 1-98) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The amino acid sequence numbering follows the bovine scheme, with the first four residues given negative values. These four residues are disordered and not included in the coordinates. |
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Sample preparation
Details |
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Sample conditions | Ionic strength: low / pH: 6.2 / Pressure: ambient / Temperature: 298 K | |||||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: distance geometry simulated annealing, molecular dynamics Software ordinal: 1 Details: His 26, 27, 39, 63, and 80 were protonated at the NE2 position in accordance to 15N NMR data. His 15 has a high pK and was protonated at the ND1 and NE2 positions. Additional details are ...Details: His 26, 27, 39, 63, and 80 were protonated at the NE2 position in accordance to 15N NMR data. His 15 has a high pK and was protonated at the ND1 and NE2 positions. Additional details are provided in the primary citation. | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 1 |