[English] 日本語
![](img/lk-miru.gif)
- PDB-1rne: THE CRYSTAL STRUCTURE OF RECOMBINANT GLYCOSYLATED HUMAN RENIN ALO... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1rne | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | THE CRYSTAL STRUCTURE OF RECOMBINANT GLYCOSYLATED HUMAN RENIN ALONE AND IN COMPLEX WITH A TRANSITION STATE ANALOG INHIBITOR | |||||||||
![]() | RENIN | |||||||||
![]() | HYDROLASE(ACID PROTEINASE) | |||||||||
Function / homology | ![]() 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 / amyloid-beta metabolic process ...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 / amyloid-beta metabolic process / Metabolism of Angiotensinogen to Angiotensins / cell maturation / response to cAMP / hormone-mediated signaling pathway / kidney development / insulin-like growth factor receptor binding / 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 | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Gruetter, M.G. / Rahuel, J. / Priestle, J.P. | |||||||||
![]() | ![]() 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: ![]() 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: ![]() 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 79.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 62 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 507.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 523.2 KB | Display | |
Data in XML | ![]() | 10.9 KB | Display | |
Data in CIF | ![]() | 16.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
| ||||||||
Atom site foot note | 1: RESIDUES PRO 23, PRO 111, PRO 294, AND PRO 297 ARE CIS PROLINES. | ||||||||
Components on special symmetry positions |
|
-
Components
#1: Protein | Mass: 37267.008 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
---|---|
#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: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.03 Å3/Da / Density % sol: 59.42 % | |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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
|
-Data collection
Radiation | Scattering type: x-ray |
---|---|
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 |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Rfactor obs: 0.176 / Highest resolution: 2.4 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.4 Å
| ||||||||||||
Software | *PLUS Name: CORELS / Classification: refinement | ||||||||||||
Refine LS restraints | *PLUS
|