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Open data
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Basic information
Entry | Database: PDB / ID: 1ldt | ||||||
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Title | COMPLEX OF LEECH-DERIVED TRYPTASE INHIBITOR WITH PORCINE TRYPSIN | ||||||
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![]() | COMPLEX (HYDROLASE/INHIBITOR) / COMPLEX (HYDROLASE-INHIBITOR) / HYDROLASE / INHIBITOR / INFLAMMATION / TRYPTASE / COMPLEX (HYDROLASE-INHIBITOR) complex | ||||||
Function / homology | ![]() trypsin / digestion / serine-type endopeptidase inhibitor activity / serine-type endopeptidase activity / proteolysis / extracellular space / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Stubbs, M.T. | ||||||
![]() | ![]() Title: The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition. Authors: Stubbs, M.T. / Morenweiser, R. / Sturzebecher, J. / Bauer, M. / Bode, W. / Huber, R. / Piechottka, G.P. / Matschiner, G. / Sommerhoff, C.P. / Fritz, H. / Auerswald, E.A. #1: ![]() Title: Structure of Leech Derived Tryptase Inhibitor (Ldti-C) in Solution Authors: Muhlhahn, P. / Czisch, M. / Morenweiser, R. / Habermann, B. / Engh, R.A. / Sommerhoff, C.P. / Auerswald, E.A. / Holak, T.A. #2: ![]() Title: Recombinant Leech-Derived Tryptase Inhibitor: Construction, Production, Protein Chemical Characterization and Inhibition of HIV-1 Replication Authors: Auerswald, E.A. / Morenweiser, R. / Sommerhoff, C.P. / Piechottka, G.P. / Eckerskorn, C. / Gurtler, L.G. / Fritz, H. #3: ![]() Title: A Kazal-Type Inhibitor of Human Mast Cell Tryptase: Isolation from the Medical Leech Hirudo Medicinalis, Characterization, and Sequence Analysis Authors: Sommerhoff, C.P. / Sollner, C. / Mentele, R. / Piechottka, G.P. / Auerswald, E.A. / Fritz, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 67.5 KB | Display | ![]() |
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PDB format | ![]() | 48.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424.7 KB | Display | ![]() |
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Full document | ![]() | 427.6 KB | Display | |
Data in XML | ![]() | 13.3 KB | Display | |
Data in CIF | ![]() | 18.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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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Components on special symmetry positions |
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Components
#1: Protein | Mass: 23493.496 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: Protein/peptide | Mass: 4750.614 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: LEECH-DERIVED TRYPTASE INHIBITOR / Source: (gene. exp.) ![]() ![]() ![]() |
#3: Chemical | ChemComp-CA / |
#4: Water | ChemComp-HOH / |
Compound details | THIS STRUCTURE OF LDTI IN COMPLEX WITH TRYPSIN REVEALS STRUCTURAL ASPECTS OF THE MAST CELL ...THIS STRUCTURE OF LDTI IN COMPLEX WITH TRYPSIN REVEALS STRUCTURAL |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.28 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 / Details: 10% PEG 6000, 2.3M PHOSPHATE, PH 8.0 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 1, 1995 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→20 Å / Num. obs: 21466 / % possible obs: 98.6 % / Observed criterion σ(I): 2 / Redundancy: 6.5 % / Rmerge(I) obs: 0.082 / Rsym value: 0.082 / Net I/σ(I): 9 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.2 / Mean I/σ(I) obs: 4 / Rsym value: 0.2 / % possible all: 87.6 |
Reflection | *PLUS Num. measured all: 139563 |
Reflection shell | *PLUS % possible obs: 87.6 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PORCINE TRYPSIN MODEL FROM TRYPSIN:MUNG BEAN INHIBITOR (LIN ET AL., EUR. J. BIOCHEM. 212, 549-555 (1993) Resolution: 1.9→6 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / σ(F): 0 Details: THE LDTI MOIETY IS WELL DEFINED IN THE VICINITY OF THE PROTEINASE, BUT IS CHARACTERIZED BY ELEVATED TEMPERATURE FACTORS AND DISRUPTED DENSITY FURTHER AWAY FROM TRYPSIN. IN PARTICULAR, AMINO ...Details: THE LDTI MOIETY IS WELL DEFINED IN THE VICINITY OF THE PROTEINASE, BUT IS CHARACTERIZED BY ELEVATED TEMPERATURE FACTORS AND DISRUPTED DENSITY FURTHER AWAY FROM TRYPSIN. IN PARTICULAR, AMINO ACID RESIDUES LYS L 1I - LYS L 2I, GLY L 15 I - ARG L 19I, SER L 33I - SER L 36I AND THE C-TERMINAL RESIDUES PRO L 41I - ASN L 46I ARE DEFINED BY EITHER WEAK OR NO ELECTRON DENSITY. ACCORDINGLY, THE COORDINATES FOR PRO L 41I - ASN L 46I ARE NOT RELIABLE.
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Refine analyze | Luzzati d res low obs: 6 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.93 Å / Total num. of bins used: 20
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 21 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor obs: 0.29 |