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- PDB-2alp: REFINED STRUCTURE OF ALPHA-LYTIC PROTEASE AT 1.7 ANGSTROMS RESOLU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2alp | |||||||||
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Title | REFINED STRUCTURE OF ALPHA-LYTIC PROTEASE AT 1.7 ANGSTROMS RESOLUTION. ANALYSIS OF HYDROGEN BONDING AND SOLVENT STRUCTURE | |||||||||
![]() | ALPHA-LYTIC PROTEASE | |||||||||
![]() | HYDROLASE (SERINE PROTEINASE) | |||||||||
Function / homology | ![]() alpha-lytic endopeptidase / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Fujinaga, M. / Delbaere, L.T.J. / Brayer, G.D. / James, M.N.G. | |||||||||
![]() | ![]() 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. #1: ![]() 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. #2: ![]() Title: Comparison of the Predicted Model of Alph-Lytic Protease with the X-Ray Structure Authors: Delbaere, L.T.J. / Brayer, G.D. / James, M.N.G. #3: ![]() Title: Amino Acid Sequence Alignment of Bacterial and Mammalian Pancreatic Serine Proteases Based on Topological Equivalences Authors: James, M.N.G. / Delbaere, L.T.J. / Brayer, G.D. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 50.3 KB | Display | ![]() |
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PDB format | ![]() | 35.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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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Atom site foot note | 1: RESIDUE 95 IS A CIS-PROLINE. |
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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: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.55 Å3/Da / Density % sol: 51.7 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 6.1 / Method: microdialysis / Details: Brayer, G.D., (1979) J.Mol.Biol., 131, 743. | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS |
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Processing
Refinement | Resolution: 1.7→8 Å / Rfactor Rwork: 0.131 / σ(I): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement step | Cycle: LAST / Resolution: 1.7→8 Å
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Refine LS restraints |
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Refinement | *PLUS Num. reflection obs: 14996 / σ(I): 2 / Highest resolution: 1.7 Å / Lowest resolution: 8 Å / Rfactor obs: 0.131 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 14.3 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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