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- PDB-1p03: STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1p03 | ||||||
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Title | STRUCTURE ANALYSIS OF SPECIFICITY. ALPHA-LYTIC PROTEASE COMPLEXES WITH ANALOGUES OF REACTION INTERMEDIATES | ||||||
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![]() | HYDROLASE/HYDROLASE INHIBITOR / 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 analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates. Authors: Bone, R. / Frank, D. / Kettner, C.A. / Agard, D.A. #1: ![]() Title: Structural Plasticity as a Determinant of Enzyme Specificity. Creating Broadly Specific Proteases Authors: Bone, R. / Silen, J.L. / 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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PDBx/mmCIF format | ![]() | 52.8 KB | Display | ![]() |
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PDB format | ![]() | 37 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 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 | 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: 2.52 Å3/Da / Density % sol: 51.22 % | ||||||||||||||||||
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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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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Highest resolution: 2.15 Å |
Reflection | *PLUS % possible obs: 89 % |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Rfactor obs: 0.142 / Highest resolution: 2.15 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: 2.15 Å
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Refinement | *PLUS σ(I): 3 / Highest resolution: 2.15 Å / Rfactor obs: 0.142 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS Type: p_bond_d / Dev ideal: 0.14 |