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Yorodumi- PDB-1lsg: THREE-DIMENSIONAL STRUCTURE OF THE PLATELET INTEGRIN RECOGNITION ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lsg | ||||||
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Title | THREE-DIMENSIONAL STRUCTURE OF THE PLATELET INTEGRIN RECOGNITION SEGMENT OF THE FIBRINOGEN GAMMA CHAIN OBTAINED BY CARRIER PROTEIN-DRIVEN CRYSTALLIZATION | ||||||
Components | HEN EGG WHITE LYSOZYME | ||||||
Keywords | HYBRID PROTEIN / LYSOZYME / FIBRINOGEN | ||||||
Function / homology | Function and homology information Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / defense response to bacterium ...Antimicrobial peptides / Neutrophil degranulation / beta-N-acetylglucosaminidase activity / cell wall macromolecule catabolic process / lysozyme / lysozyme activity / killing of cells of another organism / defense response to Gram-negative bacterium / defense response to Gram-positive bacterium / defense response to bacterium / endoplasmic reticulum / extracellular space / identical protein binding / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Patel, H. / Anderson, W.F. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1994 Title: Three-dimensional structure of the platelet integrin recognition segment of the fibrinogen gamma chain obtained by carrier protein-driven crystallization. Authors: Donahue, J.P. / Patel, H. / Anderson, W.F. / Hawiger, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lsg.cif.gz | 34.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lsg.ent.gz | 26.9 KB | Display | PDB format |
PDBx/mmJSON format | 1lsg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ls/1lsg ftp://data.pdbj.org/pub/pdb/validation_reports/ls/1lsg | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CYS 128 - ARG 129 OMEGA = 138.19 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
-Components
#1: Protein | Mass: 15892.904 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Gene: CDNA / Organ: EGG / Plasmid: PNED7 / Production host: Escherichia coli (E. coli) / References: UniProt: P00698 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.62 % | ||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 22 ℃ / pH: 2.5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Num. obs: 4625 / % possible obs: 90 % |
Reflection | *PLUS Highest resolution: 2.4 Å / Num. measured all: 15024 / Rmerge(I) obs: 0.14 |
-Processing
Software |
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Refinement | Resolution: 2.4→15 Å / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.4→15 Å
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