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Open data
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Basic information
Entry | Database: PDB / ID: 1fax | ||||||
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Title | COAGULATION FACTOR XA INHIBITOR COMPLEX | ||||||
![]() | (FACTOR XA![]() | ||||||
![]() | ![]() ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Brandstetter, H. / Engh, R.A. | ||||||
![]() | ![]() Title: X-ray structure of active site-inhibited clotting factor Xa. Implications for drug design and substrate recognition. Authors: Brandstetter, H. / Kuhne, A. / Bode, W. / Huber, R. / von der Saal, W. / Wirthensohn, K. / Engh, R.A. #1: ![]() Title: X-Ray Structure of Clotting Factor Ixa: Active Site and Module Structure Related to Xase Activity and Hemophilia B Authors: Brandstetter, H. / Bauer, M. / Huber, R. / Lollar, P. / Bode, W. #2: ![]() Title: Structure of Human Des(1-45) Factor Xa at 2.2 A Resolution Authors: Padmanabhan, K. / Padmanabhan, K.P. / Tulinsky, A. / Park, C.H. / Bode, W. / Huber, R. / Blankenship, D.T. / Cardin, A.D. / Kisiel, W. #3: ![]() Title: A Novel Factor Xa Inhibitor: Structure-Activity Relationships and Selectivity between Factor Xa and Thrombin Authors: Katakura, S. / Nagahara, T. / Hara, T. / Iwamoto, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 79.4 KB | Display | ![]() |
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PDB format | ![]() | 63.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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: 28435.510 Da / Num. of mol.: 1 Mutation: PROTEOLYTIC CLEAVAGE PRODUCT, GLA DOMAIN, RESIDUES 1 - 44 OF THE LIGHT CHAIN, ARE REMOVED Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein | ![]() Mass: 10490.688 Da / Num. of mol.: 1 Mutation: PROTEOLYTIC CLEAVAGE PRODUCT, GLA DOMAIN, RESIDUES 1 - 44 OF THE LIGHT CHAIN, ARE REMOVED Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Chemical | ChemComp-CA / |
#4: Chemical | ChemComp-DX9 / ( |
Compound details | EGF1 DOMAIN IS DISORDERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.84 % | ||||||||||||||||||||||||
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Crystal grow![]() | *PLUS pH: 5.8 / Method: unknown | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Sep 15, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Observed criterion σ(I): 3 / Redundancy: 5.6 % / Rmerge(I) obs: 0.118 |
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Processing
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Refinement | Highest resolution: 3 Å / σ(F): 2
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Refinement step | Cycle: LAST / Highest resolution: 3 Å /
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Refine LS restraints |
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