+
Open data
-
Basic information
| Entry | Database: PDB / ID: 9dzk | |||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | Human GC-A bound to REGN5308 | |||||||||||||||||||||
Components |
| |||||||||||||||||||||
Keywords | MEMBRANE PROTEIN / receptor | |||||||||||||||||||||
| Function / homology | Function and homology informationANPR-A receptor complex / natriuretic peptide receptor activity / : / receptor guanylyl cyclase signaling pathway / body fluid secretion / peptide receptor activity / positive regulation of renal sodium excretion / guanylate cyclase / cGMP biosynthetic process / guanylate cyclase activity ...ANPR-A receptor complex / natriuretic peptide receptor activity / : / receptor guanylyl cyclase signaling pathway / body fluid secretion / peptide receptor activity / positive regulation of renal sodium excretion / guanylate cyclase / cGMP biosynthetic process / guanylate cyclase activity / Physiological factors / regulation of vascular permeability / positive regulation of urine volume / G protein-coupled peptide receptor activity / : / dopamine metabolic process / hormone binding / peptide hormone binding / negative regulation of angiogenesis / blood vessel diameter maintenance / negative regulation of smooth muscle cell proliferation / negative regulation of cell growth / regulation of blood pressure / cell surface receptor signaling pathway / protein kinase activity / receptor complex / GTP binding / ATP binding / plasma membrane Similarity search - Function | |||||||||||||||||||||
| Biological species | Homo sapiens (human)![]() | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||||||||||||||
Authors | Liu, S. / Huang, X.-Y. | |||||||||||||||||||||
| Funding support | United States, 1items
| |||||||||||||||||||||
Citation | Journal: To Be PublishedTitle: human NPR1 bound to RGN5308 Authors: Liu, S. / Huang, X.-Y. | |||||||||||||||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 9dzk.cif.gz | 243.9 KB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb9dzk.ent.gz | 171.8 KB | Display | PDB format |
| PDBx/mmJSON format | 9dzk.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dz/9dzk ftp://data.pdbj.org/pub/pdb/validation_reports/dz/9dzk | HTTPS FTP |
|---|
-Related structure data
| Related structure data | ![]() 47332MC M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
-Protein , 1 types, 2 molecules BA
| #1: Protein | Mass: 115702.828 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NPR1, ANPRA / Production host: ![]() |
|---|
-Antibody , 2 types, 2 molecules HL
| #2: Antibody | Mass: 24468.420 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
|---|---|
| #3: Antibody | Mass: 23323.898 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
-Sugars , 3 types, 8 molecules 
| #4: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Polysaccharide | Source method: isolated from a genetically manipulated source #7: Sugar | ChemComp-NAG / |
|---|
-Non-polymers , 2 types, 3 molecules 


| #6: Chemical | | #8: Water | ChemComp-HOH / | |
|---|
-Details
| Has ligand of interest | Y |
|---|---|
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: Complex of Guanylyl Cyclase-A/Natriuretic peptide receptor A with Fab fragment Type: COMPLEX / Entity ID: #1-#3 / Source: RECOMBINANT |
|---|---|
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 8 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Vitrification | Cryogen name: ETHANE |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-
Processing
| EM software | Name: PHENIX / Version: 1.20.1_4487: / Category: model refinement | ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 291000 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
|
Movie
Controller
About Yorodumi




Homo sapiens (human)

United States, 1items
Citation




PDBj










FIELD EMISSION GUN