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Open data
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Basic information
Entry | Database: PDB / ID: 3n89 | ||||||
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Title | KH domains | ||||||
![]() | Defective in germ line development protein 3, isoform a | ||||||
![]() | CELL CYCLE / KH domains / RNA binding / germline development | ||||||
Function / homology | ![]() germ-line sex determination / polynucleotide adenylyltransferase activator activity / masculinization of hermaphroditic germ-line / vulval development / nematode larval development / germ-line stem cell division / RNA-directed RNA polymerase complex / positive regulation of meiosis I / nuclear division / positive regulation of meiotic nuclear division ...germ-line sex determination / polynucleotide adenylyltransferase activator activity / masculinization of hermaphroditic germ-line / vulval development / nematode larval development / germ-line stem cell division / RNA-directed RNA polymerase complex / positive regulation of meiosis I / nuclear division / positive regulation of meiotic nuclear division / positive regulation of multicellular organism growth / cytosolic mRNA polyadenylation / P granule / embryo development ending in birth or egg hatching / RNA polymerase complex / : / mitotic cytokinesis / positive regulation of mitotic nuclear division / meiotic cell cycle / mRNA processing / regulation of translation / spermatogenesis / protein domain specific binding / positive regulation of gene expression / perinuclear region of cytoplasm / RNA binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Nakel, K. / Hartung, S.A. / Bonneau, F. / Eckmann, C.R. / Conti, E. | ||||||
![]() | ![]() Title: Four KH domains of the C. elegans Bicaudal-C ortholog GLD-3 form a globular structural platform. Authors: Nakel, K. / Hartung, S.A. / Bonneau, F. / Eckmann, C.R. / Conti, E. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 143.9 KB | Display | ![]() |
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PDB format | ![]() | 112.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.9 KB | Display | ![]() |
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Full document | ![]() | 457.2 KB | Display | |
Data in XML | ![]() | 26.5 KB | Display | |
Data in CIF | ![]() | 35.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 42876.961 Da / Num. of mol.: 2 / Fragment: UNP residues 88-460 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.48 Å3/Da / Density % sol: 64.62 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7 Details: Ammoniumsulfate, Hepes, Glycerol, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
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Radiation |
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Reflection | Resolution: 2.79→48.1 Å / Num. obs: 28664 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.7 % / Rsym value: 0.134 / Net I/σ(I): 8.61 | ||||||||||||||||||
Reflection shell | Resolution: 2.79→3.07 Å / Redundancy: 2.5 % / Mean I/σ(I) obs: 2.3 / Num. unique all: 7600 / Rsym value: 0.593 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Bsol: 50.023 Å2 | ||||||||||||||||||||||||||||
Displacement parameters | Biso max: 59.8 Å2 / Biso mean: 31.207 Å2 / Biso min: 10.19 Å2
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Refinement step | Cycle: LAST / Resolution: 2.789→48.113 Å
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Refine LS restraints |
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Xplor file |
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