+Open data
-Basic information
Entry | Database: PDB / ID: 2x0b | ||||||
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Title | Crystal structure of human angiotensinogen complexed with renin | ||||||
Components |
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Keywords | HYDROLASE/HORMONE / HYDROLASE-HORMONE COMPLEX / HYDROLASE HORMONE COMPLEX / VASOCONSTRICTOR / GLYCOPROTEIN / HYPERTENSION / SERPINS / ZYMOGEN / HYDROLASE / VASOACTIVE | ||||||
Function / homology | Function and homology information regulation of blood volume by renin-angiotensin / response to muscle activity involved in regulation of muscle adaptation / regulation of renal sodium excretion / : / type 2 angiotensin receptor binding / maintenance of blood vessel diameter homeostasis by renin-angiotensin / negative regulation of neurotrophin TRK receptor signaling pathway / regulation of extracellular matrix assembly / positive regulation of activation of Janus kinase activity / renin ...regulation of blood volume by renin-angiotensin / response to muscle activity involved in regulation of muscle adaptation / regulation of renal sodium excretion / : / type 2 angiotensin receptor binding / maintenance of blood vessel diameter homeostasis by renin-angiotensin / negative regulation of neurotrophin TRK receptor signaling pathway / regulation of extracellular matrix assembly / positive regulation of activation of Janus kinase activity / renin / regulation of renal output by angiotensin / positive regulation of NAD(P)H oxidase activity / juxtaglomerular apparatus development / mesonephros development / response to cGMP / G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger / renin-angiotensin regulation of aldosterone production / renal system process / drinking behavior / positive regulation of branching involved in ureteric bud morphogenesis / positive regulation of CoA-transferase activity / positive regulation of extracellular matrix assembly / positive regulation of macrophage derived foam cell differentiation / low-density lipoprotein particle remodeling / vasoconstriction / type 1 angiotensin receptor binding / response to angiotensin / positive regulation of extrinsic apoptotic signaling pathway / positive regulation of epidermal growth factor receptor signaling pathway / positive regulation of cardiac muscle hypertrophy / positive regulation of gap junction assembly / regulation of MAPK cascade / regulation of vasoconstriction / response to immobilization stress / regulation of cardiac conduction / angiotensin maturation / positive regulation of epithelial to mesenchymal transition / blood vessel remodeling / positive regulation of protein tyrosine kinase activity / Metabolism of Angiotensinogen to Angiotensins / amyloid-beta metabolic process / nitric oxide mediated signal transduction / cell maturation / response to cAMP / insulin-like growth factor receptor binding / positive regulation of protein metabolic process / hormone-mediated signaling pathway / Peptide ligand-binding receptors / negative regulation of MAP kinase activity / positive regulation of endothelial cell migration / kidney development / regulation of cell growth / positive regulation of cytokine production / angiotensin-activated signaling pathway / growth factor activity / serine-type endopeptidase inhibitor activity / hormone activity / PPARA activates gene expression / regulation of blood pressure / positive regulation of inflammatory response / positive regulation of miRNA transcription / male gonad development / positive regulation of reactive oxygen species metabolic process / positive regulation of fibroblast proliferation / cellular response to xenobiotic stimulus / cell-cell signaling / apical part of cell / phospholipase C-activating G protein-coupled receptor signaling pathway / positive regulation of NF-kappaB transcription factor activity / regulation of cell population proliferation / peptidase activity / G alpha (i) signalling events / G alpha (q) signalling events / collagen-containing extracellular matrix / blood microparticle / regulation of apoptotic process / response to lipopolysaccharide / aspartic-type endopeptidase activity / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / G protein-coupled receptor signaling pathway / signaling receptor binding / positive regulation of DNA-templated transcription / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.33 Å | ||||||
Authors | Zhou, A. / Wei, Z. / Yan, Y. / Carrell, R.W. / Read, R.J. | ||||||
Citation | Journal: Nature / Year: 2010 Title: A Redox Switch in Angiotensinogen Modulates Angiotensin Release. Authors: Zhou, A. / Carrell, R.W. / Murphy, M.P. / Wei, Z. / Yan, Y. / Stanley, P.L. / Stein, P.E. / Pipkin, F.B. / Read, R.J. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2x0b.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2x0b.ent.gz | 1 MB | Display | PDB format |
PDBx/mmJSON format | 2x0b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x0/2x0b ftp://data.pdbj.org/pub/pdb/validation_reports/x0/2x0b | HTTPS FTP |
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-Related structure data
Related structure data | 2wxwSC 2wxxC 2wxyC 2wxzC 2wy0C 2wy1C C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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4 |
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Unit cell |
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-Components
#1: Protein | Mass: 42364.020 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PSUMO3-HANGT / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P00797, renin #2: Protein | Mass: 49807.844 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: HUMAN ANGIOTENSINOGEN / Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PSUMO3-HANGT / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P01019 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 6 Å3/Da / Density % sol: 79 % / Description: NONE |
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Crystal grow | pH: 6 / Details: 1.6-2.2M AS, 0.1M MES, PH6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.979 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 31, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 4.35→50.5 Å / Num. obs: 6793 / % possible obs: 97.2 % / Observed criterion σ(I): 2 / Redundancy: 2.4 % / Biso Wilson estimate: 170.03 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 3.6 |
Reflection shell | Resolution: 4.35→4.59 Å / Redundancy: 2 % / Rmerge(I) obs: 0.86 / Mean I/σ(I) obs: 1 / % possible all: 89.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2WXW Resolution: 4.33→48.52 Å / SU ML: 0.82 / σ(F): 1.96 / Phase error: 41.6 / Stereochemistry target values: ML Details: STRUCTURE WAS SOLVED BY MOLECULAR REPLACEMENT. VERY LIMITED REBUILDING WAS CARRIED OUT. IT WAS CLEAR FROM ELECTRON DENSITY THAT THE N-TERMINAL SUBSTRATE PORTION OF ANGIOTENSINOGEN WAS BOUND ...Details: STRUCTURE WAS SOLVED BY MOLECULAR REPLACEMENT. VERY LIMITED REBUILDING WAS CARRIED OUT. IT WAS CLEAR FROM ELECTRON DENSITY THAT THE N-TERMINAL SUBSTRATE PORTION OF ANGIOTENSINOGEN WAS BOUND IN THE ACTIVE SITE. THIS WAS MODELED BY SUPERIMPOSING THE STRUCTURE OF 1SMR, CHANGING THE SIDE CHAINS AND ADJUSTING THE ROTAMERS. RESIDUES CORRESPONDING TO 3-5 AND 15- 18 OF ANGIOTENSINOGEN WERE ADDED, ROUGHLY FITTING THEM TO THE DENSITY. DIFFERENCE DENSITY AND DENSITY OBTAINED BY AVERAGING THE FOUR COPIES IN COOT MADE IT CLEAR THAT THE LOOP 127-143 OF ANGIOTENSINOGEN HAD TO CHANGE CONFORMATION TO AVOID SERIOUS CLASHES WITH RENIN. THIS LOOP WAS REBUILT TO ROUGHLY FOLLOW THE DENSITY, BUT THE DETAILS OF ITS CONFORMATION WILL NOT BE RELIABLE. THIS IS WHY THERE ARE SERIOUS CLASHES IN THIS PORTION
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 197.49 Å2 / ksol: 0.29 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 4.33→48.52 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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