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Yorodumi- PDB-2ren: STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ren | ||||||
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Title | STRUCTURE OF RECOMBINANT HUMAN RENIN, A TARGET FOR CARDIOVASCULAR-ACTIVE DRUGS, AT 2.5 ANGSTROMS RESOLUTION | ||||||
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 / cell maturation / response to immobilization stress / 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 / cell maturation / response to immobilization stress / amyloid-beta metabolic process / hormone-mediated signaling pathway / angiotensin maturation / Metabolism of Angiotensinogen to Angiotensins / response to cAMP / insulin-like growth factor receptor binding / kidney development / regulation of blood pressure / cellular response to xenobiotic stimulus / male gonad development / apical part of cell / peptidase activity / aspartic-type endopeptidase activity / response to lipopolysaccharide / signaling receptor binding / proteolysis / extracellular space / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.5 Å | ||||||
Authors | Sielecki, A.R. / James, M.N.G. | ||||||
Citation | Journal: Science / Year: 1989 Title: Structure of recombinant human renin, a target for cardiovascular-active drugs, at 2.5 A resolution. Authors: Sielecki, A.R. / Hayakawa, K. / Fujinaga, M. / Murphy, M.E. / Fraser, M. / Muir, A.K. / Carilli, C.T. / Lewicki, J.A. / Baxter, J.D. / James, M.N. | ||||||
History |
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Remark 700 | SHEET THE C-TERMINAL DOMAIN HAS MORE STRANDS THAT ARE NOT FORMALLY HYDROGEN BONDED TO OTHER STRANDS ...SHEET THE C-TERMINAL DOMAIN HAS MORE STRANDS THAT ARE NOT FORMALLY HYDROGEN BONDED TO OTHER STRANDS TO FORM A SHEET. THERE ARE ALSO A FEW IN THE N-TERMINAL DOMAIN. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ren.cif.gz | 71 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ren.ent.gz | 55.4 KB | Display | PDB format |
PDBx/mmJSON format | 2ren.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ren_validation.pdf.gz | 391.4 KB | Display | wwPDB validaton report |
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Full document | 2ren_full_validation.pdf.gz | 417.7 KB | Display | |
Data in XML | 2ren_validation.xml.gz | 11.5 KB | Display | |
Data in CIF | 2ren_validation.cif.gz | 16 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/re/2ren ftp://data.pdbj.org/pub/pdb/validation_reports/re/2ren | HTTPS FTP |
-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: CIS PROLINE - PRO 29 / 2: CIS PROLINE - PRO 308 / 3: CIS PROLINE - PRO 311 4: ATOMS IN THE FOLLOWING RESIDUES HAVE BEEN ASSIGNED A TEMPERATURE FACTOR OF 99.99 INDICATING THAT THE ASSOCIATED ELECTRON DENSITY IS VERY POOR: ARG 82 - GLY 86 SER 213 - THR 214 ALA 248 - ASP 254 |
-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) / References: UniProt: P00797, renin |
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#2: Sugar | ChemComp-NAG / |
Sequence details | THE HUMAN RENIN GENE HAS BEEN SEQUENCED BY TWO GROUPS: 1. HOBART ET AL. (1984) PNAS, V. 81, P. 5026 ...THE HUMAN RENIN GENE HAS BEEN SEQUENCED BY TWO GROUPS: 1. HOBART ET AL. (1984) PNAS, V. 81, P. 5026 2. HARDMAN ET AL. (1984) DNA, V. 3, P. 457 THE EXON5-EXON6 JUNCTION IN 2. HAS A 9 BASE EXON CODING FOR AN ASP-SER-GLU TRIPEPTIDE |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51.39 % | ||||||||||||||||||
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Crystal grow | *PLUS pH: 4.7 / Method: batch method | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 8 Å / Num. obs: 13343 / Num. measured all: 60512 / Rmerge(I) obs: 0.48 |
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-Processing
Software |
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Refinement | Resolution: 2.5→8 Å / σ(F): 1 Details: ATOMS IN THE FOLLOWING RESIDUES HAVE BEEN ASSIGNED A TEMPERATURE FACTOR OF 99.99 INDICATING THAT THE ASSOCIATED ELECTRON DENSITY IS VERY POOR: ARG 82 - GLY 86 SER 213 - THR 214 ALA 248 - ASP 254
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Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 8 Å / Num. reflection obs: 13614 / σ(F): 1 / Rfactor obs: 0.217 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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