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Open data
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Basic information
Entry | Database: PDB / ID: 1luc | ||||||
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Title | BACTERIAL LUCIFERASE | ||||||
![]() | (BACTERIAL LUCIFERASE) x 2 | ||||||
![]() | FLAVOPROTEIN / MONOOXYGENASE | ||||||
Function / homology | ![]() bacterial luciferase / alkanal monooxygenase (FMN-linked) activity / bioluminescence / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Fisher, A.J. / Rayment, I. | ||||||
![]() | ![]() Title: The 1.5-A resolution crystal structure of bacterial luciferase in low salt conditions. Authors: Fisher, A.J. / Thompson, T.B. / Thoden, J.B. / Baldwin, T.O. / Rayment, I. #1: ![]() Title: Three-Dimensional Structure of Bacterial Luciferase from Vibrio Harveyi at 2.4 A Resolution Authors: Fisher, A.J. / Raushel, F.M. / Baldwin, T.O. / Rayment, I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 155.5 KB | Display | ![]() |
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PDB format | ![]() | 119.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 391.8 KB | Display | ![]() |
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Full document | ![]() | 406.7 KB | Display | |
Data in XML | ![]() | 15.3 KB | Display | |
Data in CIF | ![]() | 26.6 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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Unit cell |
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Components
#1: Protein | Mass: 40197.062 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Protein | Mass: 36384.684 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
#3: Chemical | #4: Chemical | ChemComp-EDO / #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.21 Å3/Da / Density % sol: 44 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 6.5 / Method: batch method | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→30 Å / Num. obs: 105012 / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Rmerge(I) obs: 0.041 |
Reflection | *PLUS Num. obs: 105158 / % possible obs: 99 % / Num. measured all: 297839 |
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Processing
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Refinement | Resolution: 1.5→30 Å / σ(F): 0 /
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Displacement parameters | Biso mean: 22.2 Å2 | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→30 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 105018 / Rfactor obs: 0.182 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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