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- PDB-1p12: CRYSTAL STRUCTURES OF ALPHA-LYTIC PROTEASE COMPLEXES WITH IRREVER... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1p12 | |||||||||
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Title | CRYSTAL STRUCTURES OF ALPHA-LYTIC PROTEASE COMPLEXES WITH IRREVERSIBLY BOUND PHOSPHONATE ESTERS | |||||||||
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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: Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters. Authors: Bone, R. / Sampson, N.S. / Bartlett, P.A. / Agard, D.A. #1: ![]() Title: Peptidic Phosphonylating Agents as Irreversible Inhibitors of Serine Proteases and Models of the Tetrahedral Intermediates Authors: Sampson, N.S. / Bartlett, P.A. #2: ![]() 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. #3: ![]() 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 | ![]() | 56.1 KB | Display | ![]() |
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PDB format | ![]() | 38.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 385.4 KB | Display | ![]() |
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Full document | ![]() | 391.1 KB | Display | |
Data in XML | ![]() | 6.5 KB | Display | |
Data in CIF | ![]() | 10.4 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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Atom site foot note | 1: PRO E 99A IS A CIS PROLINE. / 2: SEE REMARK 5. / 3: SEE REMARK 6. |
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Components
#1: Protein | Mass: 19875.131 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 | THE PVA RESIDUE IN THE INHIBITOR IS THE ALPHA-AMINO PHOSPHONIC ACID ANALOG OF VAL IN WHICH THE C- ...THE PVA RESIDUE IN THE INHIBITOR IS THE ALPHA-AMINO PHOSPHONIC |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.51 Å3/Da / Density % sol: 50.95 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7.2 / Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Rfactor obs: 0.124 / Highest resolution: 1.9 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 1.9 Å
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Refine LS restraints | *PLUS
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