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- PDB-1boq: PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRIT... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1boq | ||||||
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Title | PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE | ||||||
![]() | PROTEIN (ALPHA-LYTIC PROTEASE) | ||||||
![]() | HYDROLASE / SERINE PROTEASE / FOLDING MUTANT | ||||||
Function / homology | ![]() alpha-lytic endopeptidase / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Peters, R.J. / Shiau, A.K. / Sohl, J.L. / Anderson, D.E. / Tang, G. / Silen, J.L. / Agard, D.A. | ||||||
![]() | ![]() Title: Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease. Authors: Peters, R.J. / Shiau, A.K. / Sohl, J.L. / Anderson, D.E. / Tang, G. / Silen, J.L. / Agard, D.A. #1: ![]() Title: Structural Basis for Broad Specificity in Alpha-Lytic Protease Authors: Bone, R. / Fujishige, A. / Kettner, C.A. / Agard, D.A. #2: ![]() Title: Structural Plasticity Broadens the Specificity of an Engineered Protease Authors: Bone, R. / Silen, J.L. / Agard, D.A. #3: ![]() Title: Structural Analysis of Specificity: Alpha-Lytic Protease Complexes with Analogues of Reaction Intermediates Authors: Bone, R. / Frank, D. / Kettner, C.A. / Agard, D.A. #4: ![]() Title: Serine Protease Mechanism: Structure of an Inhibitory Complex of Alpha-Lytic Protease and a Tightly Bound Peptide Boronic Acid Authors: Bone, R. / Shenvi, A.B. / Kettner, C.A. / Agard, D.A. #5: ![]() Title: Refined Structure of Alpha-Lytic Protease at 1.7 A Resolution. Analysis of Hydrogen Bonding and Solvent Structure Authors: Fujinaga, M. / Delbaere, L.T. / Brayer, G.D. / James, M.N. #6: ![]() Title: Molecular Structure of the Alpha-Lytic Protease from Myxobacter 495 at 2.8 Angstroms Resolution Authors: Brayer, G.D. / Delbaere, L.T. / James, M.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 51.7 KB | Display | ![]() |
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PDB format | ![]() | 35.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 375.3 KB | Display | ![]() |
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Full document | ![]() | 377 KB | Display | |
Data in XML | ![]() | 5.6 KB | Display | |
Data in CIF | ![]() | 8.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2alpS S: Starting model for refinement |
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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: 19889.156 Da / Num. of mol.: 1 / Mutation: V119I / Source method: isolated from a natural source / Source: (natural) ![]() | ||||
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#2: Chemical | #3: Water | ChemComp-HOH / | Sequence details | RESIDUE NUMBERING IS BY HOMOLOGY WITH CHYMOTRYPS | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 48.2 % |
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Crystal grow | pH: 8 / Details: pH 8.0 |
Crystal grow | *PLUS pH: 6.8 / Method: vapor diffusion, hanging drop / Details: ambient temperature |
Components of the solutions | *PLUS Conc.: 1.3 M / Common name: lithium sulfate |
-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 25, 1992 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. obs: 33422 / % possible obs: 99 % / Observed criterion σ(I): -3 / Redundancy: 4.7 % / Rmerge(I) obs: 0.059 |
Reflection shell | Resolution: 2.2→2.2 Å / % possible all: 99.1 |
Reflection shell | *PLUS % possible obs: 99.1 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2ALP Resolution: 2.1→6 Å / Cross valid method: FREE R / σ(F): 0
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Displacement parameters | Biso mean: 15.2 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→6 Å
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Refine LS restraints |
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