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Yorodumi- PDB-1p09: STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CRE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1p09 | ||||||
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Title | STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES | ||||||
Components | ALPHA-LYTIC PROTEASEAlpha-lytic endopeptidase | ||||||
Keywords | HYDROLASE (SERINE PROTEINASE) | ||||||
Function / homology | Function and homology information alpha-lytic endopeptidase / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | Lysobacter enzymogenes (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.2 Å | ||||||
Authors | Bone, R. / Agard, D.A. | ||||||
Citation | Journal: Nature / Year: 1989 Title: Structural plasticity broadens the specificity of an engineered protease. Authors: Bone, R. / Silen, J.L. / Agard, D.A. #1: Journal: To be Published 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: Journal: Biochemistry / Year: 1988 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: Journal: Biochemistry / Year: 1987 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: Journal: J.Mol.Biol. / Year: 1985 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: Journal: J.Mol.Biol. / Year: 1979 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1p09.cif.gz | 47.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1p09.ent.gz | 36.7 KB | Display | PDB format |
PDBx/mmJSON format | 1p09.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p0/1p09 ftp://data.pdbj.org/pub/pdb/validation_reports/p0/1p09 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUE 99A IS A CIS-PROLINE. |
-Components
#1: Protein | Mass: 19815.014 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Lysobacter enzymogenes (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P00778, alpha-lytic endopeptidase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.57 Å3/Da / Density % sol: 52.05 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 6.8 / Method: vapor diffusion, hanging dropDetails: seeding, refer to Bone, R. et al (1987). Biochemistry, 27, 7609-7614. | ||||||||||||||||||
Components of the solutions | *PLUS
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-Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Rfactor obs: 0.135 / Highest resolution: 2.2 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.2 Å
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Refinement | *PLUS Highest resolution: 2.2 Å / σ(I): 3 / Rfactor obs: 0.135 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS Type: p_bond_d / Dev ideal: 0.09 |