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- PDB-2uwo: Selective and Dual Action Orally Active Inhibitors of Thrombin an... -
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Basic information
Entry | Database: PDB / ID: 2uwo | ||||||
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Title | Selective and Dual Action Orally Active Inhibitors of Thrombin and Factor Xa | ||||||
![]() | (COAGULATION FACTOR X) x 2 | ||||||
![]() | HYDROLASE / TARGET HOPPING / SERINE PROTEASE / EGF-LIKE DOMAIN / POLYMORPHISM / GLYCOPROTEIN / HYDROXYLATION / CALCIUM / ZYMOGEN / COMPLEX / PROTEASE / BLOOD COAGULATION / GAMMA- CARBOXYGLUTAMIC ACID / CLEAVAGE ON PAIR OF BASIC RESIDUES | ||||||
Function / homology | ![]() 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 | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Young, R.J. / Brown, D. / Burns-Kurtis, C.L. / Chan, C. / Convery, M.A. / Hubbard, J.A. / Kelly, H.A. / Pateman, A.J. / Patikis, A. / Senger, S. ...Young, R.J. / Brown, D. / Burns-Kurtis, C.L. / Chan, C. / Convery, M.A. / Hubbard, J.A. / Kelly, H.A. / Pateman, A.J. / Patikis, A. / Senger, S. / Shah, G.P. / Toomey, J.R. / Watson, N.S. / Zhou, P. | ||||||
![]() | ![]() Title: Selective and Dual Action Orally Active Inhibitors of Thrombin and Factor Xa. Authors: Young, R.J. / Brown, D. / Burns-Kurtis, C.L. / Chan, C. / Convery, M.A. / Hubbard, J.A. / Kelly, H.A. / Pateman, A.J. / Patikis, A. / Senger, S. / Shah, G.P. / Toomey, J.R. / Watson, N.S. / Zhou, P. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 79.4 KB | Display | ![]() |
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PDB format | ![]() | 57.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2uwlC ![]() 2uwpC ![]() 1ezqS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 28550.596 Da / Num. of mol.: 1 / Fragment: ACTIVATED DESGLA, RESIDUES 235-488 / Source method: isolated from a natural source Details: PURCHASED FROM ENZYME RESEARCH LABS. ISOLATED FROM HUMAN BLOOD Source: (natural) ![]() |
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#2: Protein | Mass: 15210.793 Da / Num. of mol.: 1 / Fragment: ACTIVATED DESGLA, RESIDUES 46-179 / Source method: isolated from a natural source Details: PURCHASED FROM ENZYME RESEARCH LABS. ISOLATED FROM HUMAN BLOOD Source: (natural) ![]() |
#3: Chemical | ChemComp-701 / ( |
#4: Water | ChemComp-HOH / |
Sequence details | SOME RESIDUES IN CHAIN ARE NOT SEEN IN THE ELECTRON DENSITY. SEQUENCE DATABASE RESIDUES 1-45 (THE ...SOME RESIDUES IN CHAIN ARE NOT SEEN IN THE ELECTRON DENSITY. SEQUENCE DATABASE RESIDUES 1-45 (THE GLA DOMAIN) WERE BIOCHEMICA |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.34 Å3/Da / Density % sol: 47.05 % |
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Crystal grow | pH: 5.75 / Details: 18% PEG6K, 50MM MES PH5.75, 10MM CACL2, 150MM NACL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Oct 8, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.93 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→20 Å / Num. obs: 33109 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 3.5 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 22.1 |
Reflection shell | Resolution: 1.75→1.81 Å / Rmerge(I) obs: 0.47 / Mean I/σ(I) obs: 2.5 / % possible all: 98.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1EZQ Resolution: 1.75→20 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.93 / SU B: 2.709 / SU ML: 0.088 / Cross valid method: THROUGHOUT / ESU R: 0.12 / ESU R Free: 0.127 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 32.78 Å2
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Refinement step | Cycle: LAST / Resolution: 1.75→20 Å
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