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Yorodumi- PDB-1lah: STRUCTURAL BASES FOR MULTIPLE LIGAND SPECIFICITY OF THE PERIPLASM... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1lah | ||||||
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Title | STRUCTURAL BASES FOR MULTIPLE LIGAND SPECIFICITY OF THE PERIPLASMIC LYSINE-, ARGININE-, ORNITHINE-BINDING PROTEIN | ||||||
Components | LYSINE, ARGININE, ORNITHINE-BINDING PROTEIN | ||||||
Keywords | AMINO ACID TRANSPORT | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Salmonella typhimurium (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.06 Å | ||||||
Authors | Kim, S.-H. / Oh, B.-H. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1994 Title: Structural basis for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein. Authors: Oh, B.H. / Ames, G.F. / Kim, S.H. #1: Journal: J.Biol.Chem. / Year: 1993 Title: Three-Dimensional Structures of the Periplasmic Lysine-, Arginine-, Ornithine-Binding Protein with and without a Ligand Authors: Oh, B.-H. / Pandit, J. / Kang, C.-H. / Nikaido, K. / Gokcen, S. / Ames, G.F.-L. / Kim, S.-H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lah.cif.gz | 56.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lah.ent.gz | 44.3 KB | Display | PDB format |
PDBx/mmJSON format | 1lah.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lah_validation.pdf.gz | 375.4 KB | Display | wwPDB validaton report |
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Full document | 1lah_full_validation.pdf.gz | 376.9 KB | Display | |
Data in XML | 1lah_validation.xml.gz | 6.4 KB | Display | |
Data in CIF | 1lah_validation.cif.gz | 9.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/la/1lah ftp://data.pdbj.org/pub/pdb/validation_reports/la/1lah | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO E 16 2: THE FOLLOWING FIVE RESIDUES HAVE BEEN MODELED AS ALANINE DUE TO THE ABSENCE OF ELECTRON DENSITY FOR THEIR SIDE CHAIN: GLN E 4, LYS E 110, LYS E 188, LYS E 189, AND LYS E 228. |
-Components
#1: Protein | Mass: 26058.314 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Salmonella typhimurium (bacteria) / References: UniProt: P02911 |
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#2: Chemical | ChemComp-ORN / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50.03 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6.5 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||
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 | *PLUS Highest resolution: 2.06 Å / % possible obs: 89.2 % / Observed criterion σ(F): 1 / Rmerge(I) obs: 0.0609 |
-Processing
Software |
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Refinement | Resolution: 2.06→6 Å / Rfactor Rwork: 0.158 / Rfactor obs: 0.158 / σ(F): 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.06→6 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 24.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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