- PDB-3ens: Crystal structure of human FXA in complex with methyl (2Z)-3-[(3-... -
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Entry
Database: PDB / ID: 3ens
Title
Crystal structure of human FXA in complex with methyl (2Z)-3-[(3-chloro-1H-indol-7-yl)amino]-2-cyano-3-{[(3S)-2-oxo-1-(2-oxo-2-pyrrolidin-1-ylethyl)azepan-3-yl]amino}acrylate
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 leukocyte chemotaxis / 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 ...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 leukocyte chemotaxis / 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 / external side of plasma membrane / endoplasmic reticulum lumen / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / extracellular region / plasma membrane Similarity search - Function
Mass: 18.015 Da / Num. of mol.: 304 / Source method: isolated from a natural source / Formula: H2O
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Details
Sequence details
THE PROTEIN, AS ISOLATED FROM HUMAN BLOOD BY ENZYME RESEARCH LABORATORIES (SOUTH BEND, IN), WAS ...THE PROTEIN, AS ISOLATED FROM HUMAN BLOOD BY ENZYME RESEARCH LABORATORIES (SOUTH BEND, IN), WAS FOUND TO BE HETEROGENEOUS BY MASS SPECTROMETRY. THE REPROTED SEQRES RECORDS INCLUDE THE RESIDUES CONSISTENT WITH THE CARBOXYPEPTIDASE B CLEAVAGE SITE TO FORM DES-GLA PROTEIN AND THE RESIDUES MODELED IN ELECTRON DENSITY. N-TERMINI OF LIGHT CHAINS (CHAINS A AND C) MODELED BASED ON 1XKA. THERE MAY BE MORE RESIDUES BEYOND THESE TERMINI.
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.44 Å3/Da / Density % sol: 49.66 %
Crystal grow
Temperature: 298 K / pH: 6.5 Details: 15-22% W/V PEG MME 5000, 0.01 M CALCIUM ACETATE, 0.35 M SODIUM ACETATE, 0.1 M LITHIUM SULFATE, 0.1 M MES, pH 6.500000, VAPOR DIFFUSION HANGING DROP, temperature 298K, VAPOR DIFFUSION, HANGING DROP
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