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- PDB-1r42: Native Human Angiotensin Converting Enzyme-Related Carboxypeptida... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1r42 | ||||||
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Title | Native Human Angiotensin Converting Enzyme-Related Carboxypeptidase (ACE2) | ||||||
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![]() | HYDROLASE / zinc metallopeptidase domain / collectrin homology domain / native or open conformation / chloride ion binding site / zinc binding site | ||||||
Function / homology | ![]() positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / positive regulation of gap junction assembly / regulation of vasoconstriction / regulation of cardiac conduction ...positive regulation of amino acid transport / angiotensin-converting enzyme 2 / positive regulation of L-proline import across plasma membrane / Hydrolases; Acting on peptide bonds (peptidases); Metallocarboxypeptidases / angiotensin-mediated drinking behavior / regulation of systemic arterial blood pressure by renin-angiotensin / tryptophan transport / positive regulation of gap junction assembly / regulation of vasoconstriction / regulation of cardiac conduction / peptidyl-dipeptidase activity / maternal process involved in female pregnancy / angiotensin maturation / Metabolism of Angiotensinogen to Angiotensins / metallocarboxypeptidase activity / carboxypeptidase activity / negative regulation of signaling receptor activity / Attachment and Entry / positive regulation of cardiac muscle contraction / regulation of cytokine production / viral life cycle / blood vessel diameter maintenance / brush border membrane / regulation of transmembrane transporter activity / negative regulation of smooth muscle cell proliferation / negative regulation of ERK1 and ERK2 cascade / cilium / metallopeptidase activity / endocytic vesicle membrane / positive regulation of reactive oxygen species metabolic process / virus receptor activity / regulation of cell population proliferation / regulation of inflammatory response / endopeptidase activity / Induction of Cell-Cell Fusion / Potential therapeutics for SARS / entry receptor-mediated virion attachment to host cell / receptor-mediated endocytosis of virus by host cell / membrane fusion / Attachment and Entry / receptor-mediated virion attachment to host cell / symbiont entry into host cell / membrane raft / apical plasma membrane / endoplasmic reticulum lumen / cell surface / extracellular space / zinc ion binding / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Towler, P. / Staker, B. / Prasad, S.G. / Menon, S. / Ryan, D. / Tang, J. / Parsons, T. / Fisher, M. / Williams, D. / Dales, N.A. ...Towler, P. / Staker, B. / Prasad, S.G. / Menon, S. / Ryan, D. / Tang, J. / Parsons, T. / Fisher, M. / Williams, D. / Dales, N.A. / Patane, M.A. / Pantoliano, M.W. | ||||||
![]() | ![]() Title: ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis. Authors: Towler, P. / Staker, B. / Prasad, S.G. / Menon, S. / Tang, J. / Parsons, T. / Ryan, D. / Fisher, M. / Williams, D. / Dales, N.A. / Patane, M.A. / Pantoliano, M.W. #1: ![]() Title: Substrate-based design of the first class of angiotensin-converting enzyme-related carboxypeptidase (ACE2) inhibitors Authors: A Dales, N. / Gould, A.E. / Brown, J.A. / Calderwood, E.F. / Guan, B. / Minor, C.A. / Gavin, J.M. / Hales, P. / Kaushik, V.K. / Stewart, M. / Tummino, P.J. / Vickers, C.S. / Ocain, T.D. / Pantane, M.A. #2: ![]() Title: Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase Authors: Vickers, C. / Hales, P. / Kaushik, V. / Dick, L. / Gavin, J. / Tang, J. / Godbout, K. / Parsons, T. / Baronas, E. / Hsieh, F. / Acton, S. / Patane, M. / Nichols, A. / Tummino, P. | ||||||
History |
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Remark 999 | SEQUENCE The complete sequence crystallized by the authors (residues 1-740 of reference sequence GB ...SEQUENCE The complete sequence crystallized by the authors (residues 1-740 of reference sequence GB 11225609) is as follows: MSSSSWLLLSLVAVTAAQSTIEEQAKTFLDKFNHEAEDLFYQSSLASWNY NTNITEENVQNMNNAGDKWSAFLKEQSTLAQMYPLQEIQNLTVKLQLQALQ QNGSSVLSEDKSKRLNTILNTMSTIYSTGKVCNPDNPQECLLLEPGLNEIM ANSLDYNERLWAWESWRSEVGKQLRPLYEEYVVLKNEMARANHYEDYGDYW RGDYEVNGVDGYDYSRGQLIEDVEHTFEEIKPLYEHLHAYVRAKLMNAYPS YISPIGCLPAHLLGDMWGRFWTNLYSLTVPFGQKPNIDVTDAMVDQAWDAQ RIFKEAEKFFVSVGLPNMTQGFWENSMLTDPGNVQKAVCHPTAWDLGKGDF RILMCTKVTMDDFLTAHHEMGHIQYDMAYAAQPFLLRNGANEGFHEAVGEI MSLSAATPKHLKSIGLLSPDFQEDNETEINFLLKQALTIVGTLPFTYMLEK WRWMVFKGEIPKDQWMKKWWEMKREIVGVVEPVPHDETYCDPASLFHVSND YSFIRYYTRTLYQFQFQEALCQAAKHEGPLHKCDISNSTEAGQKLFNMLRL GKSEPWTLALENVVGAKNMNVRPLLNYFEPLFTWLKDQNKNSFVGWSTDWS PYADQSIKVRISLKSALGDKAYEWNDNEMYLFRSSVAYAMRQYFLKVKNQ MILFGEEDVRVANLKPRISFNFFVTAPKNVSDIIPRTEVEKAIRMSRSRIN DAFRLNDNSLEFLGIQPTLGPPNQPPVS The electron density map for much of the collectrin homology domain (residues 616-740) is weak. Only about half of this domain was visible in the electron density map, and what can be seen is ambiguous due to topology and connectivity issues. For this reason, residues beginning at 901 are labeled as unknown (UNK). Each fragment of unknown residues has been assigned a unique chain ID. However, it should be understood that only one sequence (residues 1-740) was crystallized. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 145.9 KB | Display | ![]() |
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PDB format | ![]() | 117.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 474 KB | Display | ![]() |
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Full document | ![]() | 502.6 KB | Display | |
Data in XML | ![]() | 30.6 KB | Display | |
Data in CIF | ![]() | 43.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
-Disordered segment of collectrin homology ... , 4 types, 4 molecules BCDE
#2: Protein/peptide | Mass: 528.644 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#3: Protein/peptide | Mass: 1720.111 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#4: Protein/peptide | Mass: 1549.902 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#5: Protein/peptide | Mass: 1209.482 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
-Protein / Sugars , 2 types, 4 molecules A![](data/chem/img/NAG.gif)
![](data/chem/img/NAG.gif)
#1: Protein | Mass: 70999.820 Da / Num. of mol.: 1 / Fragment: Extracellular domains Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#6: Sugar |
-Non-polymers , 3 types, 304 molecules ![](data/chem/img/CL.gif)
![](data/chem/img/ZN.gif)
![](data/chem/img/HOH.gif)
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![](data/chem/img/HOH.gif)
#7: Chemical | ChemComp-CL / |
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#8: Chemical | ChemComp-ZN / |
#9: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.24 Å3/Da / Density % sol: 53 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 100 mM Tris-HCl, 200 mM MgCl2, 14% PEG 8000, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 16-18 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 140 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: AREA DETECTOR / Date: Jun 21, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.28 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→40 Å / Num. obs: 49286 / % possible obs: 96.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 15.9 % / Biso Wilson estimate: 52.8 Å2 / Rsym value: 0.057 / Net I/σ(I): 21.4 |
Reflection | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 46.7 Å / Num. obs: 47465 / Rmerge(I) obs: 0.057 |
Reflection shell | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 2.34 Å / % possible obs: 81.8 % / Num. unique obs: 5982 / Rmerge(I) obs: 0.408 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 64.5529 Å2 / ksol: 0.341723 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 59.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.2→46.74 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Lowest resolution: 46.7 Å | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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