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Open data
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Basic information
Entry | Database: PDB / ID: 1tlx | ||||||
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Title | THERMOLYSIN (NATIVE) | ||||||
![]() | THERMOLYSIN | ||||||
![]() | HYDROLASE / METALLOPROTEINASE / ORGANIC SOLVENT | ||||||
Function / homology | ![]() thermolysin / metalloendopeptidase activity / proteolysis / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | English, A.C. / Done, S.H. / Groom, C.R. / Hubbard, R.E. | ||||||
![]() | ![]() Title: Locating interaction sites on proteins: the crystal structure of thermolysin soaked in 2% to 100% isopropanol. Authors: English, A.C. / Done, S.H. / Caves, L.S. / Groom, C.R. / Hubbard, R.E. #1: ![]() Title: Structural Analysis of Zinc Substitutions in the Active Site of Thermolysin Authors: Holland, D.R. / Hausrath, A.C. / Juers, D. / Matthews, B.W. #2: ![]() Title: Structure of Thermolysin Refined at 1.6 Angstrom Resolution Authors: Holmes, M.A. / Matthews, B.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 79.6 KB | Display | ![]() |
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PDB format | ![]() | 59.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 468.4 KB | Display | ![]() |
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Full document | ![]() | 472.7 KB | Display | |
Data in XML | ![]() | 15.5 KB | Display | |
Data in CIF | ![]() | 22.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1tliC ![]() 2tliC ![]() 2tlxC ![]() 3tliC ![]() 4tliC ![]() 5tliC ![]() 6tliC ![]() 7tliC ![]() 8tliC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 34362.305 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Non-polymers , 6 types, 154 molecules ![](data/chem/img/VAL.gif)
![](data/chem/img/LYS.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/LYS.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/DMS.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-VAL / | ||||
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#3: Chemical | ChemComp-LYS / | ||||
#4: Chemical | ChemComp-ZN / | ||||
#5: Chemical | ChemComp-CA / #6: Chemical | ChemComp-DMS / | #7: Water | ChemComp-HOH / | |
-Details
Compound details | THE ACTIVE SITE CLEFT OF THERMOLYSINonpolymer details | RESIDUES 317 AND 318 FORM A DIPEPTIDE (VAL-LYS) BOUND IN THE ACTIVE SITE OF THE MOLECULE. IT IS ...RESIDUES 317 AND 318 FORM A DIPEPTIDE (VAL-LYS) BOUND IN THE ACTIVE SITE OF THE MOLECULE. IT IS PRESUMED THAT THE ORIGIN OF THIS DIPEPTIDE IS THE C-TERMINAL TWO RESIDUES OF THE PROTEIN. SINCE THE C-TERMINUS APPEARS AT FULL OCCUPANCY, MOLECULES NOT INCORPORAT | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 49 % |
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Crystal grow | pH: 7.5 / Details: pH 7.5 |
Crystal grow | *PLUS Method: unknownDetails: This particular structure is not described in this paper. |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Dec 1, 1996 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. obs: 20252 / % possible obs: 99 % / Redundancy: 14.9 % / Rmerge(I) obs: 0.123 / Net I/σ(I): 4.9 |
Reflection shell | Resolution: 2.1→2.24 Å / Redundancy: 15 % / Rmerge(I) obs: 0.386 / Mean I/σ(I) obs: 2 / % possible all: 98 |
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Processing
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Refinement | Method to determine structure: ISOMORPHOUS REPLACEMENT / Resolution: 2.1→20 Å / SU B: 3.5 / SU ML: 0.1 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.18 / ESU R Free: 0.17 Details: THIS ENTRY FORMS PART OF A SERIES OF STRUCTURES GENERATED FROM SOAKING CRYSTALS OF THERMOLYSIN IN ORGANIC SOLVENTS/ SOLUTES. THIS ENTRY WAS USED AS THE INITIAL MODEL FOR THE REFINEMENT OF THESE STRUCTURES.
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Displacement parameters | Biso mean: 25.18 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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Refine LS restraints |
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