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Open data
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Basic information
Entry | Database: PDB / ID: 1bx8 | ||||||
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Title | HIRUSTASIN FROM HIRUDO MEDICINALIS AT 1.4 ANGSTROMS | ||||||
![]() | HIRUSTASIN | ||||||
![]() | ANTI-COAGULANT / PEPTIDIC INHIBITORS / CONFORMATIONAL FLEXIBILITY / SERINE PROTEASE INHIBITOR | ||||||
Function / homology | ![]() negative regulation of coagulation / serine-type endopeptidase inhibitor activity / heparin binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Uson, I. / Sheldrick, G.M. / De La Fortelle, E. / Bricogne, G. / Di Marco, S. / Priestle, J.P. / Gruetter, M.G. / Mittl, P.R.E. | ||||||
![]() | ![]() Title: The 1.2 A crystal structure of hirustasin reveals the intrinsic flexibility of a family of highly disulphide-bridged inhibitors. Authors: Uson, I. / Sheldrick, G.M. / de La Fortelle, E. / Bricogne, G. / Di Marco, S. / Priestle, J.P. / Grutter, M.G. / Mittl, P.R. #1: ![]() Title: A New Structural Class of Serine Protease Inhibitors Revealed by the Structure of the Hirustasin-Kallikrein Complex Authors: Mittl, P.R. / Di Marco, S. / Fendrich, G. / Pohlig, G. / Heim, J. / Sommerhoff, C. / Fritz, H. / Priestle, J.P. / Grutter, M.G. #2: ![]() Title: Recombinant Hirustasin: Production in Yeast, Crystallization, and Interaction with Serine Proteases Authors: Di Marco, S. / Fendrich, G. / Knecht, R. / Strauss, A. / Pohlig, G. / Heim, J. / Priestle, J.P. / Sommerhoff, C.P. / Grutter, M.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 | ![]() | 27.6 KB | Display | ![]() |
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PDB format | ![]() | 17.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 404.2 KB | Display | ![]() |
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Full document | ![]() | 404.2 KB | Display | |
Data in XML | ![]() | 3.3 KB | Display | |
Data in CIF | ![]() | 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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Components
#1: Protein | Mass: 5886.788 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 40 % Description: TWO DIFFERENT INDEPENDENT METHODS WERE USED FOR STRUCTURE SOLUTION | ||||||||||||||||||||||||
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Crystal grow | pH: 5.45 / Details: pH 5.45 | ||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown / Details: Di Marco, S., (1997) Protein Sci., 6, 109. | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jun 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→7.1 Å / Num. obs: 10468 / % possible obs: 98.6 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 50.5 |
Reflection shell | Resolution: 1.4→1.45 Å / Rmerge(I) obs: 0.376 / Mean I/σ(I) obs: 8.5 / % possible all: 73.4 |
Reflection | *PLUS Redundancy: 6.8 % |
Reflection shell | *PLUS % possible obs: 97.7 % / Rmerge(I) obs: 0.174 / Mean I/σ(I) obs: 3.4 |
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Processing
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Refinement | Method to determine structure: AB INITIO / Resolution: 1.4→7.1 Å / Num. parameters: 1641 / Num. restraintsaints: 1470 / Cross valid method: FREE R / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER Details: ANISOTROPIC REFINEMENT OF THE SULPHUR ATOMS REDUCED FREE R (NO CUTOFF) BY 1%.
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Solvent computation | Solvent model: MOEWS & KRETSINGER, J.MOL.BIOL.91(1973)201-2 | |||||||||||||||||||||||||||||||||
Refine analyze | Num. disordered residues: 1 / Occupancy sum hydrogen: 323 / Occupancy sum non hydrogen: 390.5 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.4→7.1 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL-97 / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.178 / Rfactor obs: 0.1648 / Rfactor Rwork: 0.1768 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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