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Open data
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Basic information
Entry | Database: PDB / ID: 1kj5 | ||||||
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Title | Solution Structure of Human beta-defensin 1 | ||||||
![]() | BETA-DEFENSIN 1 | ||||||
![]() | ANTIBIOTIC / Defensin / antimicrobial protein / human beta-defensin 1 / beta-defensin / HBD1 | ||||||
Function / homology | ![]() positive regulation of flagellated sperm motility involved in capacitation / microvesicle / CCR6 chemokine receptor binding / Beta defensins / Defensins / : / sperm midpiece / cAMP-mediated signaling / innate immune response in mucosa / response to bacterium ...positive regulation of flagellated sperm motility involved in capacitation / microvesicle / CCR6 chemokine receptor binding / Beta defensins / Defensins / : / sperm midpiece / cAMP-mediated signaling / innate immune response in mucosa / response to bacterium / Golgi lumen / antimicrobial humoral immune response mediated by antimicrobial peptide / chemotaxis / antibacterial humoral response / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / defense response to bacterium / immune response / G protein-coupled receptor signaling pathway / innate immune response / extracellular space / extracellular exosome / extracellular region / identical protein binding / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / distance geometry, simulated annealing, molecular dynamics | ||||||
![]() | Schibli, D.J. / Hunter, H.N. / Aseyev, V. / Starner, T.D. / Wiencek, J.M. / McCray Jr., P.B. / Tack, B.F. / Vogel, H.J. | ||||||
![]() | ![]() Title: The solution structures of the human beta-defensins lead to a better understanding of the potent bactericidal activity of HBD3 against Staphylococcus aureus. Authors: Schibli, D.J. / Hunter, H.N. / Aseyev, V. / Starner, T.D. / Wiencek, J.M. / McCray Jr., P.B. / Tack, B.F. / Vogel, H.J. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 208.2 KB | Display | ![]() |
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PDB format | ![]() | 179.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 336.2 KB | Display | ![]() |
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Full document | ![]() | 445.8 KB | Display | |
Data in XML | ![]() | 12.4 KB | Display | |
Data in CIF | ![]() | 20.1 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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1 |
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 3940.598 Da / Num. of mol.: 1 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: This structure was determined using standard 2D homonuclear techniques. |
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Sample preparation
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Sample conditions | pH: 3.79 / Pressure: ambient / Temperature: 298 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
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Refinement | Method: distance geometry, simulated annealing, molecular dynamics Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |