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- PDB-1p10: STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CRE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1p10 | ||||||
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Title | STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / SERINE PROTEINASE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | ![]() alpha-lytic endopeptidase / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Bone, R. / Agard, D.A. | ||||||
![]() | ![]() Title: Structural plasticity broadens the specificity of an engineered protease. Authors: Bone, R. / Silen, J.L. / Agard, D.A. #1: ![]() Title: Structure Analysis of Specificity. Alpha-Lytic Protease Complexes with Analogues of Reaction Intermediates Authors: Bone, R. / Frank, D. / Kettner, C. / Agard, D.A. #2: ![]() Title: Kinetic Properties of the Binding of Alpha-Lytic Protease to Peptide Boronic Acids Authors: Kettner, C.A. / Bone, R. / Agard, D.A. / Bachovchin, W.W. #3: ![]() 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. #4: ![]() Title: Refined Structure of Alpha-Lytic Protease at 1.7 Angstroms Resolution. Analysis of Hydrogen Bonding and Solvent Structure Authors: Fujinaga, M. / Delbaere, L.T.J. / Brayer, G.D. / James, M.N.G. #5: ![]() Title: Molecular Structure of the Alpha-Lytic Protease from Myxobacter 495 at 2.8 Angstroms Resolution Authors: Brayer, G.D. / Delbaere, L.T.J. / James, M.N.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 53.4 KB | Display | ![]() |
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PDB format | ![]() | 37.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 386 KB | Display | ![]() |
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Full document | ![]() | 392.7 KB | Display | |
Data in XML | ![]() | 6.5 KB | Display | |
Data in CIF | ![]() | 9.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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
#1: Protein | Mass: 19815.014 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | |
#3: Chemical | ChemComp-SO4 / |
#4: Water | ChemComp-HOH / |
Compound details | INHIBITORY PEPTIDE BORONIC ACIDS ARE PEPTIDE ANALOGS IN WHICH THE C-TERMINAL CARBOXYL GROUP HAS ...INHIBITORY |
Nonpolymer details | INHIBITORY PEPTIDE BORONIC ACIDS ARE PEPTIDE ANALOGUES IN WHICH THE C-TERMINAL CARBOXY GROUP (COOH) ...INHIBITORY |
Sequence details | CHAIN A RESIDUE NUMBERING IS DONE BY HOMOLOGY WITH CHYMOTRYPSIN FOR RESIDUES 15A - 244 AS DESCRIBED ...CHAIN A RESIDUE NUMBERING IS DONE BY HOMOLOGY WITH CHYMOTRYPS |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.29 % |
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Highest resolution: 2.25 Å |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Rfactor obs: 0.144 / Highest resolution: 2.25 Å Details: THE METHOXYSUCCINYL PORTION OF THE INHIBITOR WAS DISORDERED AND NO COORDINATES ARE INCLUDED FOR IT IN THIS ENTRY | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.25 Å
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Refinement | *PLUS Highest resolution: 2.25 Å / Rfactor obs: 0.144 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |