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- PDB-1fxy: COAGULATION FACTOR XA-TRYPSIN CHIMERA INHIBITED WITH D-PHE-PRO-AR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1fxy | ||||||
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Title | COAGULATION FACTOR XA-TRYPSIN CHIMERA INHIBITED WITH D-PHE-PRO-ARG-CHLOROMETHYLKETONE | ||||||
![]() | COAGULATION FACTOR XA-TRYPSIN CHIMERA | ||||||
![]() | hydrolase/hydrolase inhibitor / CHIMERA / PROTEASE / CHLOROMETHYLKETONE / HYDROLASE-HYDROLASE INHIBITOR COMPLEX | ||||||
Function / homology | ![]() Uptake of dietary cobalamins into enterocytes / Activation of Matrix Metalloproteinases / trypsin / extracellular matrix disassembly / digestion / collagen-containing extracellular matrix / blood microparticle / serine-type endopeptidase activity / proteolysis / extracellular space ...Uptake of dietary cobalamins into enterocytes / Activation of Matrix Metalloproteinases / trypsin / extracellular matrix disassembly / digestion / collagen-containing extracellular matrix / blood microparticle / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Hopfner, K.P. / Kopetzki, E. / Kresse, G.-B. / Huber, R. / Bode, W. / Engh, R.A. | ||||||
![]() | ![]() Title: New enzyme lineages by subdomain shuffling. Authors: Hopfner, K.P. / Kopetzki, E. / Kresse, G.B. / Bode, W. / Huber, R. / Engh, R.A. | ||||||
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 KB | Display | ![]() |
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PDB format | ![]() | 49.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 443 KB | Display | ![]() |
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Full document | ![]() | 443.2 KB | Display | |
Data in XML | ![]() | 5.9 KB | Display | |
Data in CIF | ![]() | 8.8 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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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 24668.814 Da / Num. of mol.: 1 / Mutation: Q20Y, E21N, C27V Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-0G6 / |
#3: Water | ChemComp-HOH / |
Nonpolymer details | THE UNBOUND FORM OF THE INHIBITOR IS D-PHE-PRO-ARG-CHLOROMETHYLKETONE. UPON REACTION WITH PROTEIN ...THE UNBOUND FORM OF THE INHIBITOR IS D-PHE-PRO-ARG-CHLOROMETH |
Sequence details | RESIDUES ARE NUMBERED ACCORDING TO THE CHYMOTRYPSIN NUMBERING SYSTEM. THE MOLECULE IS A CHIMERIC ...RESIDUES ARE NUMBERED ACCORDING TO THE CHYMOTRYPS |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 46.13 % | ||||||||||||||||||||
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Crystal grow | pH: 7.8 Details: PROTEIN WAS CRYSTALLIZED FROM 15% PEG 6K, 100 MM HEPES, PH 7.8. | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, sitting drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 280 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 1, 1995 |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Highest resolution: 2.15 Å |
Reflection | *PLUS Lowest resolution: 8 Å / Num. obs: 10714 / % possible obs: 89.3 % / Rmerge(I) obs: 0.072 / Num. measured all: 28062 |
Reflection shell | *PLUS Highest resolution: 2.15 Å / Lowest resolution: 2.25 Å / % possible obs: 91.6 % |
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Processing
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Refinement | Resolution: 2.15→8 Å / Data cutoff high absF: 1000000 / Data cutoff low absF: 0.001 / Cross valid method: FREE R-VALUE / σ(F): 2
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Refinement step | Cycle: LAST / Resolution: 2.15→8 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.185 / Rfactor Rfree: 0.241 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 1.2 |