[English] 日本語
Yorodumi- PDB-4jzd: Structure of factor VIIA in complex with the inhibitor 2-{2-[(4-c... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4jzd | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of factor VIIA in complex with the inhibitor 2-{2-[(4-carbamimidoylphenyl)carbamoyl]-6-methoxypyridin-3-yl}-5-{[(2S)-1-hydroxy-3,3-dimethylbutan-2-yl]carbamoyl}benzoic acid | ||||||
Components |
| ||||||
Keywords | HYDROLASE/HYDROLASE INHIBITOR / glycoprotein / serine protease / plasma / blood coagulation factor / protein inhibitor complex / calcium binding / HYDROLASE-HYDROLASE INHIBITOR complex | ||||||
Function / homology | Function and homology information coagulation factor VIIa / response to Thyroid stimulating hormone / response to 2,3,7,8-tetrachlorodibenzodioxine / response to astaxanthin / response to thyrotropin-releasing hormone / response to genistein / serine-type peptidase complex / positive regulation of platelet-derived growth factor receptor signaling pathway / response to vitamin K / response to carbon dioxide ...coagulation factor VIIa / response to Thyroid stimulating hormone / response to 2,3,7,8-tetrachlorodibenzodioxine / response to astaxanthin / response to thyrotropin-releasing hormone / response to genistein / serine-type peptidase complex / positive regulation of platelet-derived growth factor receptor signaling pathway / response to vitamin K / response to carbon dioxide / response to thyroxine / response to cholesterol / response to growth hormone / positive regulation of positive chemotaxis / Extrinsic Pathway of Fibrin Clot Formation / positive regulation of leukocyte chemotaxis / positive regulation of TOR signaling / positive regulation of blood coagulation / animal organ regeneration / Gamma-carboxylation of protein precursors / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / Removal of aminoterminal propeptides from gamma-carboxylated proteins / serine-type peptidase activity / BMAL1:CLOCK,NPAS2 activates circadian gene expression / protein processing / Golgi lumen / circadian rhythm / response to estrogen / blood coagulation / response to estradiol / collagen-containing extracellular matrix / vesicle / response to hypoxia / positive regulation of cell migration / endoplasmic reticulum lumen / signaling receptor binding / serine-type endopeptidase activity / calcium ion binding / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.2 Å | ||||||
Authors | Jacobson, B.L. / Anumula, R. | ||||||
Citation | Journal: Bioorg.Med.Chem.Lett. / Year: 2013 Title: Discovery of nonbenzamidine factor VIIa inhibitors using a biaryl acid scaffold. Authors: Bolton, S.A. / Sutton, J.C. / Anumula, R. / Bisacchi, G.S. / Jacobson, B. / Slusarchyk, W.A. / Treuner, U.D. / Wu, S.C. / Zhao, G. / Pi, Z. / Sheriff, S. / Smirk, R.A. / Bisaha, S. / Cheney, ...Authors: Bolton, S.A. / Sutton, J.C. / Anumula, R. / Bisacchi, G.S. / Jacobson, B. / Slusarchyk, W.A. / Treuner, U.D. / Wu, S.C. / Zhao, G. / Pi, Z. / Sheriff, S. / Smirk, R.A. / Bisaha, S. / Cheney, D.L. / Wei, A. / Schumacher, W.A. / Hartl, K.S. / Liu, E. / Zahler, R. / Seiler, S.M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4jzd.cif.gz | 86.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4jzd.ent.gz | 63.1 KB | Display | PDB format |
PDBx/mmJSON format | 4jzd.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jz/4jzd ftp://data.pdbj.org/pub/pdb/validation_reports/jz/4jzd | HTTPS FTP |
---|
-Related structure data
Related structure data | 4jzeC 4jzfC 1danS C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Components on special symmetry positions |
|
-Components
-Protein , 2 types, 2 molecules HL
#1: Protein | Mass: 28103.256 Da / Num. of mol.: 1 / Fragment: UNP residues 213-466 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: F7 / Production host: Cricetinae (hamsters) / References: UniProt: P08709, coagulation factor VIIa |
---|---|
#2: Protein | Mass: 6030.827 Da / Num. of mol.: 1 / Fragment: UNP residues 150-204 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: F7 / Production host: Cricetinae (hamsters) / References: UniProt: P08709, coagulation factor VIIa |
-Non-polymers , 5 types, 307 molecules
#3: Chemical | #4: Chemical | ChemComp-CA / | #5: Chemical | ChemComp-SO4 / #6: Chemical | ChemComp-GOL / | #7: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.9 Å3/Da / Density % sol: 68.48 % |
---|---|
Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 100 mM bicine, pH 9.0, 1.4-1.9 M lithium sulfate, 5% v/v MPD, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 / Wavelength: 1.1 Å |
Detector | Type: BRANDEIS 4 / Detector: CCD / Date: Sep 20, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 2.198→24.679 Å / Num. obs: 28001 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 4.3 % / Biso Wilson estimate: 29.69 Å2 / Rmerge(I) obs: 0.071 / Net I/σ(I): 24.8 |
Reflection shell | Resolution: 2.198→2.38 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.183 / Mean I/σ(I) obs: 8.1 / % possible all: 100 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: PDB ENTRY 1DAN Resolution: 2.2→24.679 Å / Cor.coef. Fo:Fc: 0.9486 / Cor.coef. Fo:Fc free: 0.9342 / Occupancy max: 1 / Occupancy min: 0.5 / SU R Cruickshank DPI: 0.147 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.163 / SU Rfree Blow DPI: 0.143 / SU Rfree Cruickshank DPI: 0.136 Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=CA GOL. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=2801. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=6. ...Details: IDEAL-DIST CONTACT TERM CONTACT SETUP. RESIDUE TYPES WITHOUT CCP4 ATOM TYPE IN LIBRARY=CA GOL. NUMBER OF ATOMS WITH PROPER CCP4 ATOM TYPE=2801. NUMBER WITH APPROX DEFAULT CCP4 ATOM TYPE=6. NUMBER TREATED BY BAD NON-BONDED CONTACTS=1.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 114.96 Å2 / Biso mean: 27.0992 Å2 / Biso min: 8.35 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.194 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→24.679 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.2→2.28 Å / Total num. of bins used: 14
|