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Open data
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Basic information
Entry | Database: PDB / ID: 3ljj | ||||||
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Title | Bovine trypsin in complex with UB-THR 10 | ||||||
![]() | Cationic trypsin | ||||||
![]() | HYDROLASE/HYDROLASE INHIBITOR / Metal-binding / Serine protease / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | ![]() trypsin / serpin family protein binding / serine protease inhibitor complex / digestion / endopeptidase activity / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Wegscheid-Gerlach, C. / Heine, A. / Klebe, G. | ||||||
![]() | ![]() Title: Congeneric but still distinct: how closely related trypsin ligands exhibit different thermodynamic and structural properties. Authors: Brandt, T. / Holzmann, N. / Muley, L. / Khayat, M. / Wegscheid-Gerlach, C. / Baum, B. / Heine, A. / Hangauer, D. / Klebe, 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 | ![]() | 63.3 KB | Display | ![]() |
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PDB format | ![]() | 43.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1010.7 KB | Display | ![]() |
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Full document | ![]() | 1013 KB | Display | |
Data in XML | ![]() | 7.5 KB | Display | |
Data in CIF | ![]() | 11.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2zdkC ![]() 2zdlC ![]() 2zdmC ![]() 2zdnC ![]() 2zfsC ![]() 2zftC ![]() 2zhdC ![]() 2zq1C ![]() 2zq2C ![]() 3ljoC ![]() 1k1pS C: citing same article ( S: Starting model for refinement |
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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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Components
#1: Protein | Mass: 23324.287 Da / Num. of mol.: 1 / Fragment: residues 24-246 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||
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#2: Chemical | ChemComp-10U / ( | ||
#3: Chemical | ChemComp-CA / | ||
#4: Chemical | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.91 Å3/Da / Density % sol: 57.74 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 6 Details: 1.9M Ammonium sulfate, 50mM MES, pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Aug 10, 2005 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→21.9 Å / Num. all: 39762 / Num. obs: 39762 / % possible obs: 99.2 % / Redundancy: 7.3 % / Rsym value: 0.058 / Net I/σ(I): 0.344 |
Reflection shell | Resolution: 1.55→1.58 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.364 / Mean I/σ(I) obs: 3.1 / Num. unique all: 1715 / % possible all: 88 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1K1P Resolution: 1.55→10 Å / Num. parameters: 7625 / Num. restraintsaints: 7116 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH AND HUBER Details: ANISOTROPIC SCALING APPLIED BY THE METHOD OF PARKIN, MOEZZI & HOPE, J.APPL.CRYST.28(1995)53-56
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Refine analyze | Num. disordered residues: 11 / Occupancy sum hydrogen: 1585 / Occupancy sum non hydrogen: 1857.66 | |||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.55→10 Å
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Refine LS restraints |
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