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- PDB-1g9k: CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUD... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1g9k | ||||||
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Title | CRYSTAL STRUCTURE OF A PSYCHROPHILIC ALKALINE PROTEASE FROM PSEUDOMONAS TAC II 18 | ||||||
![]() | SERRALYSIN | ||||||
![]() | HYDROLASE / beta jelly roll | ||||||
Function / homology | ![]() serralysin / extracellular matrix / metalloendopeptidase activity / calcium ion binding / proteolysis / extracellular space / zinc ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Aghajari, N. / Haser, R. | ||||||
![]() | ![]() Title: Crystal structures of a psychrophilic metalloprotease reveal new insights into catalysis by cold-adapted proteases Authors: Aghajari, N. / Van Petegem, F. / Villeret, V. / Chessa, J.P. / Gerday, C. / Haser, R. / Van Beeumen, J. #1: ![]() Title: THREE-DIMENSIONAL STRUCTURE OF THE ALKALINE PROTEASE OF PSEUDOMONAS AERUGINOSA: A TWO-DOMAIN PROTEIN WITH A CALCIUM BINDING PARALLEL BETA ROLL MOTIF Authors: Baumann, U. / Wu, S. / Flaherty, K.M. / McKay, D.B. | ||||||
History |
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Remark 999 | SEQUENCE AUTHORS CLAIM THAT THE RESIDUE 22 (33 IN SEQUENCE DATABASE) IS ASP (AND NOT GLU) AS JUDGED ...SEQUENCE AUTHORS CLAIM THAT THE RESIDUE 22 (33 IN SEQUENCE DATABASE) IS ASP (AND NOT GLU) AS JUDGED FROM ELECTRON DENSITY MAP |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 112.3 KB | Display | ![]() |
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PDB format | ![]() | 83.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 437.2 KB | Display | ![]() |
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Full document | ![]() | 438.9 KB | Display | |
Data in XML | ![]() | 21 KB | Display | |
Data in CIF | ![]() | 31.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1h71C ![]() 1kapS S: Starting model for refinement 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 48727.609 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() | ||||||
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#2: Chemical | ChemComp-CA / #3: Chemical | ChemComp-SO4 / | #4: Chemical | ChemComp-ZN / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.59 Å3/Da / Density % sol: 52.58 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: ammonium sulphate, Hepes, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 293K | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 / Details: Villeret, V., (1997) Protein Sci., 6, 2462. | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 289 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 20, 2000 / Details: mirrors |
Radiation | Monochromator: OSMIC MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.96→93.01 Å / Num. all: 34749 / Num. obs: 33263 / % possible obs: 95.7 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 4 % / Biso Wilson estimate: 16.1 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 16.1 |
Reflection shell | Resolution: 1.96→2.01 Å / Redundancy: 2 % / Rmerge(I) obs: 0.268 / Mean I/σ(I) obs: 2.7 / Num. unique all: 2029 / % possible all: 87.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: A lower resolution structure (not yet deposited) solved by the molecular replacement method using pdb entry 1KAP as a search model Resolution: 1.96→46.13 Å Isotropic thermal model: overall anisotropic B-factor correction algorithm from CNS Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 18.9 Å2 | |||||||||||||||||||||||||
Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.96→46.13 Å
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Refine LS restraints |
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Refine LS restraints | *PLUS
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