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Yorodumi- PDB-8qfx: Human Angiotensin-1 converting enzyme N-domain in complex with th... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8qfx | ||||||
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| Title | Human Angiotensin-1 converting enzyme N-domain in complex with the lactotripeptide IPP | ||||||
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Keywords | HYDROLASE / inhibitor / complex / angiotensin I coverting enzyme / metalloprotease / lactotripeptide | ||||||
| Function / homology | Function and homology informationmononuclear cell proliferation / cell proliferation in bone marrow / bradykinin receptor binding / exopeptidase activity / regulation of angiotensin metabolic process / substance P catabolic process / tripeptidyl-peptidase activity / peptidyl-dipeptidase A / regulation of renal output by angiotensin / negative regulation of gap junction assembly ...mononuclear cell proliferation / cell proliferation in bone marrow / bradykinin receptor binding / exopeptidase activity / regulation of angiotensin metabolic process / substance P catabolic process / tripeptidyl-peptidase activity / peptidyl-dipeptidase A / regulation of renal output by angiotensin / negative regulation of gap junction assembly / hormone catabolic process / bradykinin catabolic process / metallodipeptidase activity / regulation of smooth muscle cell migration / regulation of hematopoietic stem cell proliferation / neutrophil mediated immunity / hormone metabolic process / mitogen-activated protein kinase binding / mitogen-activated protein kinase kinase binding / chloride ion binding / arachidonate secretion / post-transcriptional regulation of gene expression / peptide catabolic process / heart contraction / positive regulation of systemic arterial blood pressure / regulation of heart rate by cardiac conduction / regulation of systemic arterial blood pressure by renin-angiotensin / antigen processing and presentation of peptide antigen via MHC class I / blood vessel remodeling / amyloid-beta metabolic process / hematopoietic stem cell differentiation / peptidyl-dipeptidase activity / regulation of vasoconstriction / Metabolism of Angiotensinogen to Angiotensins / angiotensin maturation / metallocarboxypeptidase activity / blood vessel diameter maintenance / angiotensin-activated signaling pathway / kidney development / regulation of synaptic plasticity / metalloendopeptidase activity / regulation of blood pressure / male gonad development / metallopeptidase activity / peptidase activity / actin binding / spermatogenesis / endopeptidase activity / calmodulin binding / lysosome / endosome / negative regulation of gene expression / external side of plasma membrane / proteolysis / extracellular space / extracellular exosome / extracellular region / zinc ion binding / plasma membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human)![]() | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.6 Å | ||||||
Authors | Gregory, K.S. / Acharya, K.R. / Cozier, G.E. | ||||||
| Funding support | United Kingdom, 1items
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Citation | Journal: Febs Lett. / Year: 2024Title: Structural insights into the inhibitory mechanism of angiotensin-I-converting enzyme by the lactotripeptides IPP and VPP. Authors: Gregory, K.S. / Cozier, G.E. / Schwager, S.L.U. / Sturrock, E.D. / Acharya, K.R. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8qfx.cif.gz | 1.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb8qfx.ent.gz | 893.1 KB | Display | PDB format |
| PDBx/mmJSON format | 8qfx.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8qfx_validation.pdf.gz | 8.1 MB | Display | wwPDB validaton report |
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| Full document | 8qfx_full_validation.pdf.gz | 8.2 MB | Display | |
| Data in XML | 8qfx_validation.xml.gz | 136.6 KB | Display | |
| Data in CIF | 8qfx_validation.cif.gz | 190.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qf/8qfx ftp://data.pdbj.org/pub/pdb/validation_reports/qf/8qfx | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8qhlC C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| 2 | ![]()
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| 3 | ![]()
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| 4 | ![]()
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| Unit cell |
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Components
-Protein / Protein/peptide , 2 types, 8 molecules ABCDEFGH
| #1: Protein | Mass: 72493.352 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ACE, DCP, DCP1 / Production host: ![]() #2: Protein/peptide | Mass: 325.403 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) ![]() |
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-Sugars , 6 types, 26 molecules 




| #3: Polysaccharide | alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose #4: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose | #5: Polysaccharide | #14: Sugar | ChemComp-NAG / #15: Sugar | ChemComp-BMA / #17: Sugar | |
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-Non-polymers , 12 types, 2380 molecules 






















| #6: Chemical | ChemComp-ZN / #7: Chemical | ChemComp-CL / #8: Chemical | ChemComp-MG / #9: Chemical | ChemComp-PGE / #10: Chemical | ChemComp-12P / | #11: Chemical | #12: Chemical | ChemComp-PEG / #13: Chemical | ChemComp-EDO / #16: Chemical | #18: Chemical | #19: Chemical | ChemComp-1PE / | #20: Water | ChemComp-HOH / | |
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-Details
| Has ligand of interest | Y |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 3.06 Å3/Da / Density % sol: 59.78 % |
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| Crystal grow | Temperature: 289.15 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 30% PEG 500 MME/PEG 20000, 0.1 M Tris/Bicine pH 8.5 and 60 mM divalent cations [Molecular Dimensions (Rotherham, UK) Morpheus A9] |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9282 Å |
| Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Dec 17, 2016 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.9282 Å / Relative weight: 1 |
| Reflection | Resolution: 1.6→114.71 Å / Num. obs: 432760 / % possible obs: 97.2 % / Redundancy: 6.9 % / CC1/2: 0.998 / Rpim(I) all: 0.061 / Net I/σ(I): 6.4 |
| Reflection shell | Resolution: 1.6→1.63 Å / Num. unique obs: 20957 / CC1/2: 0.344 / Rpim(I) all: 0.859 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.6→79.452 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.957 / SU B: 4.187 / SU ML: 0.071 / Cross valid method: FREE R-VALUE / ESU R: 0.081 / ESU R Free: 0.083
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 24.203 Å2
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| Refinement step | Cycle: LAST / Resolution: 1.6→79.452 Å
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group | Selection: ALL |
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About Yorodumi



Homo sapiens (human)
X-RAY DIFFRACTION
United Kingdom, 1items
Citation
PDBj








