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Yorodumi- PDB-1rne: THE CRYSTAL STRUCTURE OF RECOMBINANT GLYCOSYLATED HUMAN RENIN ALO... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1rne | |||||||||
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Title | THE CRYSTAL STRUCTURE OF RECOMBINANT GLYCOSYLATED HUMAN RENIN ALONE AND IN COMPLEX WITH A TRANSITION STATE ANALOG INHIBITOR | |||||||||
Components | RENIN | |||||||||
Keywords | HYDROLASE(ACID PROTEINASE) | |||||||||
Function / homology | Function and homology information renin / juxtaglomerular apparatus development / mesonephros development / response to cGMP / renin-angiotensin regulation of aldosterone production / drinking behavior / regulation of MAPK cascade / response to immobilization stress / angiotensin maturation / Metabolism of Angiotensinogen to Angiotensins ...renin / juxtaglomerular apparatus development / mesonephros development / response to cGMP / renin-angiotensin regulation of aldosterone production / drinking behavior / regulation of MAPK cascade / response to immobilization stress / angiotensin maturation / Metabolism of Angiotensinogen to Angiotensins / amyloid-beta metabolic process / cell maturation / response to cAMP / insulin-like growth factor receptor binding / hormone-mediated signaling pathway / kidney development / regulation of blood pressure / male gonad development / cellular response to xenobiotic stimulus / apical part of cell / peptidase activity / response to lipopolysaccharide / aspartic-type endopeptidase activity / signaling receptor binding / proteolysis / extracellular space / extracellular region / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | |||||||||
Authors | Gruetter, M.G. / Rahuel, J. / Priestle, J.P. | |||||||||
Citation | Journal: J.Struct.Biol. / Year: 1991 Title: The crystal structures of recombinant glycosylated human renin alone and in complex with a transition state analog inhibitor. Authors: Rahuel, J. / Priestle, J.P. / Grutter, M.G. #1: Journal: Science / Year: 1989 Title: Structure of Recombinant Human Renin, a Target for Cardiovascular-Active Drugs, at 2.5 Angstroms Resolution Authors: Sielecki, A.R. / Hayakawa, K. / Fujinaga, M. / Murphy, M.E.P. / Fraser, M. / Muir, A.K. / Carilli, C.T. / Lewicki, J.A. / Baxter, J.D. / James, M.N.G. #2: Journal: Embo J. / Year: 1989 Title: High-Resolution X-Ray Diffraction Study of the Complex between Endothiapepsin and an Oligopeptide Inhibitor: The Analysis of the Inhibitor Binding and Description of the Rigid Body Shift in the Enzyme Authors: Sali, A. / Veerapandian, B. / Cooper, J.B. / Foundling, S.I. / Hoover, D.J. / Blundell, T.L. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rne.cif.gz | 79.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rne.ent.gz | 62 KB | Display | PDB format |
PDBx/mmJSON format | 1rne.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rn/1rne ftp://data.pdbj.org/pub/pdb/validation_reports/rn/1rne | 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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Atom site foot note | 1: RESIDUES PRO 23, PRO 111, PRO 294, AND PRO 297 ARE CIS PROLINES. | ||||||||
Components on special symmetry positions |
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-Components
#1: Protein | Mass: 37267.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Organ: OVARY / References: UniProt: P00797, renin |
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#2: Sugar | ChemComp-NAG / |
#3: Chemical | ChemComp-C60 / [[[ |
#4: Water | ChemComp-HOH / |
Nonpolymer details | THE ATOMS OF NAG 345 WERE ASSIGNED OCCUPANCIES OF 0.5 TO KEEP B-FACTORS FROM GOING OVER 100 ...THE ATOMS OF NAG 345 WERE ASSIGNED OCCUPANCIE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59.42 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 3 / Method: vapor diffusion, hanging dropDetails: drop consists of equal volume of protein and reservoir solutions | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.4 Å / Num. obs: 18418 / % possible obs: 99 % / Num. measured all: 57856 / Rmerge(I) obs: 0.078 |
-Processing
Software |
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Refinement | Rfactor obs: 0.176 / Highest resolution: 2.4 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.4 Å
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Software | *PLUS Name: CORELS / Classification: refinement | ||||||||||||
Refine LS restraints | *PLUS
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