+Open data
-Basic information
Entry | Database: PDB / ID: 4aa1 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Crystal structure of ANCE in complex with Angiotensin-II | |||||||||
Components |
| |||||||||
Keywords | HYDROLASE/HORMONE / HYDROLASE-HORMONE COMPLEX / HYDROLASE / SUBSTRATE BINDING | |||||||||
Function / homology | Function and homology information Metabolism of Angiotensinogen to Angiotensins / regulation of blood volume by renin-angiotensin / response to muscle activity involved in regulation of muscle adaptation / regulation of renal sodium excretion / metamorphosis / : / type 2 angiotensin receptor binding / maintenance of blood vessel diameter homeostasis by renin-angiotensin / response to symbiotic bacterium / negative regulation of neurotrophin TRK receptor signaling pathway ...Metabolism of Angiotensinogen to Angiotensins / regulation of blood volume by renin-angiotensin / response to muscle activity involved in regulation of muscle adaptation / regulation of renal sodium excretion / metamorphosis / : / type 2 angiotensin receptor binding / maintenance of blood vessel diameter homeostasis by renin-angiotensin / response to symbiotic bacterium / negative regulation of neurotrophin TRK receptor signaling pathway / regulation of extracellular matrix assembly / peptidyl-dipeptidase A / positive regulation of activation of Janus kinase activity / regulation of renal output by angiotensin / positive regulation of NAD(P)H oxidase activity / sexual reproduction / G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger / renin-angiotensin regulation of aldosterone production / renal system process / positive regulation of branching involved in ureteric bud morphogenesis / positive regulation of macrophage derived foam cell differentiation / positive regulation of extracellular matrix assembly / vasoconstriction / positive regulation of CoA-transferase activity / low-density lipoprotein particle remodeling / type 1 angiotensin receptor binding / response to angiotensin / positive regulation of extrinsic apoptotic signaling pathway / peptide hormone processing / positive regulation of epidermal growth factor receptor signaling pathway / positive regulation of cardiac muscle hypertrophy / positive regulation of gap junction assembly / regulation of vasoconstriction / regulation of cardiac conduction / peptidyl-dipeptidase activity / positive regulation of epithelial to mesenchymal transition / blood vessel remodeling / positive regulation of protein tyrosine kinase activity / Metabolism of Angiotensinogen to Angiotensins / carboxypeptidase activity / nitric oxide mediated signal transduction / positive regulation of protein metabolic process / Peptide ligand-binding receptors / positive regulation of endothelial cell migration / negative regulation of MAP kinase activity / 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 / metallopeptidase activity / positive regulation of reactive oxygen species metabolic process / positive regulation of fibroblast proliferation / cell-cell signaling / phospholipase C-activating G protein-coupled receptor signaling pathway / positive regulation of NF-kappaB transcription factor activity / regulation of cell population proliferation / G alpha (i) signalling events / G alpha (q) signalling events / collagen-containing extracellular matrix / regulation of apoptotic process / blood microparticle / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / G protein-coupled receptor signaling pathway / positive regulation of DNA-templated transcription / proteolysis / extracellular space / extracellular exosome / extracellular region / metal ion binding / plasma membrane / cytosol Similarity search - Function | |||||||||
Biological species | DROSOPHILA MELANOGASTER (fruit fly) HOMO SAPIENS (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.99 Å | |||||||||
Authors | Isaac, R.E. / Akif, M. / Schwager, S.L.U. / Masuyer, G. / Sturrock, E.D. / Acharya, K.R. | |||||||||
Citation | Journal: FEBS J. / Year: 2012 Title: Structural Basis of Peptide Recognition by the Angiotensin-I Converting Enzyme Homologue Ance from Drosophila Melanogaster Authors: Akif, M. / Masuyer, G. / Bingham, R.J. / Sturrock, E.D. / Isaac, R.E. / Acharya, K.R. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4aa1.cif.gz | 150.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4aa1.ent.gz | 114.9 KB | Display | PDB format |
PDBx/mmJSON format | 4aa1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/aa/4aa1 ftp://data.pdbj.org/pub/pdb/validation_reports/aa/4aa1 | HTTPS FTP |
---|
-Related structure data
Related structure data | 4aa2C 4asqC 4asrC 2x8yS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
-Protein / Protein/peptide , 2 types, 2 molecules AP
#1: Protein | Mass: 69152.602 Da / Num. of mol.: 1 / Fragment: RESIDUES 17-614 Source method: isolated from a genetically manipulated source Source: (gene. exp.) DROSOPHILA MELANOGASTER (fruit fly) / Plasmid: PPIC9 / Production host: PICHIA PASTORIS (fungus) / Strain (production host): GS115 / References: UniProt: Q10714, peptidyl-dipeptidase A |
---|---|
#2: Protein/peptide | Mass: 1048.195 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P01019 |
-Sugars , 2 types, 3 molecules
#3: Polysaccharide | beta-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D- ...beta-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
---|---|
#5: Sugar |
-Non-polymers , 2 types, 552 molecules
#4: Chemical | ChemComp-ZN / |
---|---|
#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 4.3 Å3/Da / Density % sol: 71 % / Description: NONE |
---|---|
Crystal grow | pH: 7.5 / Details: 0.1 M HEPES 7.5, 1.3 M SODIUM CITRATE |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 |
Detector | Type: ADSC CCD / Detector: CCD / Date: May 9, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 1.99→50 Å / Num. obs: 78501 / % possible obs: 98.4 % / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 19 |
Reflection shell | Resolution: 1.99→2.06 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.23 / Mean I/σ(I) obs: 4 / % possible all: 91.9 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2X8Y Resolution: 1.99→38.57 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.952 / SU B: 3.15 / SU ML: 0.086 / Cross valid method: THROUGHOUT / ESU R: 0.127 / ESU R Free: 0.118 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.551 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.99→38.57 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|