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Yorodumi- PDB-2ltn: DESIGN, EXPRESSION, AND CRYSTALLIZATION OF RECOMBINANT LECTIN FRO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ltn | ||||||
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Title | DESIGN, EXPRESSION, AND CRYSTALLIZATION OF RECOMBINANT LECTIN FROM THE GARDEN PEA (PISUM SATIVUM) | ||||||
Components |
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Keywords | LECTIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Pisum sativum (garden pea) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.7 Å | ||||||
Authors | Suddath, F.L. / Phillips, S.R. / Einspahr, H. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1989 Title: Design, expression, and crystallization of recombinant lectin from the garden pea (Pisum sativum). Authors: Prasthofer, T. / Phillips, S.R. / Suddath, F.L. / Engler, J.A. #1: Journal: J.Biol.Chem. / Year: 1986 Title: The Crystal Structure of Pea Lectin at 3.0-Angstroms Resolution Authors: Einspahr, H. / Parks, E.H. / Suguna, K. / Subramanian, E. / Suddath, F.L. #2: Journal: Acta Crystallogr.,Sect.B / Year: 1985 Title: The Location of Manganese and Calcium Ion Cofactors in Pea Lectin Crystals by Use of Anomalous Dispersion and Tuneable Synchrotron X-Radiation Authors: Einspahr, H. / Suguna, K. / Suddath, F.L. / Ellis, G. / Helliwell, J.R. / Papiz, M.Z. #3: Journal: J.Biol.Chem. / Year: 1982 Title: The Crystal Structure of Pea Lectin at 6-Angstroms Resolution Authors: Meehanjunior, E.J. / Mcduffie, J. / Einspahr, H. / Bugg, C.E. / Suddath, F.L. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ltn.cif.gz | 107.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ltn.ent.gz | 82.7 KB | Display | PDB format |
PDBx/mmJSON format | 2ltn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ltn_validation.pdf.gz | 393.4 KB | Display | wwPDB validaton report |
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Full document | 2ltn_full_validation.pdf.gz | 424.8 KB | Display | |
Data in XML | 2ltn_validation.xml.gz | 14.7 KB | Display | |
Data in CIF | 2ltn_validation.cif.gz | 22.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lt/2ltn ftp://data.pdbj.org/pub/pdb/validation_reports/lt/2ltn | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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Atom site foot note | 1: THE PEPTIDE BOND BETWEEN ALA A 80 AND ASP A 81 AND THE PEPTIDE BOND BETWEEN ALA C 80 AND ASP C 81 ARE BOTH IN THE CIS CONFORMATION. |
-Components
#1: Protein | Mass: 20001.076 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pisum sativum (garden pea) / Production host: Escherichia coli (E. coli) / References: UniProt: P02867 #2: Protein | Mass: 5596.086 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pisum sativum (garden pea) / References: UniProt: P02867 #3: Chemical | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.55 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 5 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS |
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-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.177 / Highest resolution: 1.7 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.7 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.7 Å / Rfactor obs: 0.177 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |