+Open data
-Basic information
Entry | Database: PDB / ID: 1fax | ||||||
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Title | COAGULATION FACTOR XA INHIBITOR COMPLEX | ||||||
Components | (FACTOR XAFactor X) x 2 | ||||||
Keywords | COAGULATION FACTOR / GLYCOPROTEIN / HYDROLASE / SERINE PROTEASE / PLASMA / BLOOD COAGULATION FACTOR / GAMMA-CARBOXYGLUTAMIC ACID / CALCIUM-BINDING | ||||||
Function / homology | Function and homology information coagulation factor Xa / Defective factor IX causes thrombophilia / Defective cofactor function of FVIIIa variant / Defective F9 variant does not activate FX / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of TOR signaling / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins ...coagulation factor Xa / Defective factor IX causes thrombophilia / Defective cofactor function of FVIIIa variant / Defective F9 variant does not activate FX / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of TOR signaling / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Common Pathway of Fibrin Clot Formation / Removal of aminoterminal propeptides from gamma-carboxylated proteins / Intrinsic Pathway of Fibrin Clot Formation / phospholipid binding / Golgi lumen / blood coagulation / positive regulation of cell migration / endoplasmic reticulum lumen / external side of plasma membrane / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Brandstetter, H. / Engh, R.A. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1996 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: Journal: Proc.Natl.Acad.Sci.USA / Year: 1995 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: Journal: J.Mol.Biol. / Year: 1993 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: Journal: Biochem.Biophys.Res.Commun. / Year: 1993 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fax.cif.gz | 79.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fax.ent.gz | 63.1 KB | Display | PDB format |
PDBx/mmJSON format | 1fax.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fa/1fax ftp://data.pdbj.org/pub/pdb/validation_reports/fa/1fax | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-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.) Homo sapiens (human) / Tissue: BLOOD / References: UniProt: P00742, coagulation factor Xa |
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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.) Homo sapiens (human) / Tissue: BLOOD / References: UniProt: P00742, coagulation factor Xa |
#3: Chemical | ChemComp-CA / |
#4: Chemical | ChemComp-DX9 / ( |
Compound details | EGF1 DOMAIN IS DISORDERED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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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: 1.5418 Å / Relative weight: 1 |
Reflection | Observed criterion σ(I): 3 / Redundancy: 5.6 % / Rmerge(I) obs: 0.118 |
-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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