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- PDB-1tgl: A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTRE OF A TRIACYLGL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1tgl | ||||||
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Title | A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTRE OF A TRIACYLGLYCEROL LIPASE | ||||||
![]() | TRIACYL-GLYCEROL ACYLHYDROLASE | ||||||
![]() | HYDROLASE / CARBOXYLIC ESTERASE | ||||||
Function / homology | Fungal lipase-like domain / Lipase (class 3) / Lipases, serine active site. / triacylglycerol lipase / triacylglycerol lipase activity / lipid catabolic process / Alpha/Beta hydrolase fold / metal ion binding / Lipase![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Brady, L. / Brzozowski, A.M. / Derewenda, Z.S. / Dodson, E.J. / Dodson, G.G. / Tolley, S.P. / Turkenburg, J.P. / Christiansen, L. / Huge-Jensen, B. / Norskov, L. / Thim, L. | ||||||
![]() | ![]() Title: A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Authors: Brady, L. / Brzozowski, A.M. / Derewenda, Z.S. / Dodson, E. / Dodson, G. / Tolley, S. / Turkenburg, J.P. / Christiansen, L. / Huge-Jensen, B. / Norskov, L. / Thim, L. / Menge, U. #1: ![]() Title: Rhizomucor Miehei Triglyceride Lipase is Synthesized as a Precursor Authors: Boel, E. / Huge-Jensen, B. / Christensen, M. / Thim, L. / Fiil, N.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 35.3 KB | Display | ![]() |
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PDB format | ![]() | 12.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 341.6 KB | Display | ![]() |
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Full document | ![]() | 341.8 KB | Display | |
Data in XML | ![]() | 1.3 KB | Display | |
Data in CIF | ![]() | 4 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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Atom site foot note | 1: RESIDUES PRO 34, PRO 209, PRO 229, AND PRO 250 ARE CIS PROLINES. |
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Components
#1: Protein | Mass: 29508.945 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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Sequence details | RESIDUE 156 IN THIS ENTRY IS ASP AS IDENTIFIED BY ELECTRON DENSITY. IN THE PAPER CITED AS REFERENCE ...RESIDUE 156 IN THIS ENTRY IS ASP AS IDENTIFIED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.82 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.05 / 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 | *PLUS Highest resolution: 1.9 Å / Num. obs: 21165 / % possible obs: 87.8 % / Rmerge(I) obs: 0.081 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Resolution: 1.9→7.5 Å / Rfactor obs: 0.138 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→7.5 Å
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Refinement | *PLUS Num. reflection obs: 19305 / Highest resolution: 1.9 Å / Lowest resolution: 7.5 Å / Rfactor all: 0.138 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS Biso mean: 23.3 Å2 | ||||||||||||
Refine LS restraints | *PLUS
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