7FID
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![BU of 7fid by Molmil](/molmil-images/mine/7fid) | Processive cleavage of substrate at individual proteolytic active sites of the Lon proteasecomplex (conformation 1) | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, Lon protease, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... | Authors: | Li, S, Hsieh, K, Kuo, C, Su, S, Huang, K, Zhang, K, Chang, C.I. | Deposit date: | 2021-07-31 | Release date: | 2021-11-24 | Last modified: | 2024-06-12 | Method: | ELECTRON MICROSCOPY (2.44 Å) | Cite: | Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex. Sci Adv, 7, 2021
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7EV4
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![BU of 7ev4 by Molmil](/molmil-images/mine/7ev4) | Crystal structure of the Lon-like protease MtaLonC with S582A mutation in complex with F-b20-Q | Descriptor: | Endopeptidase La, F-b20-Q peptide {ortho-aminobenzoic acid (Abz)- QLRSLNGEWRFAWFPAPEAV[Tyr(3-NO2)]A}, PHOSPHATE ION | Authors: | Hsieh, K.Y, Kuo, C.I, Su, S.C, Huang, K.F, Chang, C.I. | Deposit date: | 2021-05-20 | Release date: | 2021-11-24 | Last modified: | 2023-11-29 | Method: | X-RAY DIFFRACTION (2.12 Å) | Cite: | Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex. Sci Adv, 7, 2021
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7FIZ
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![BU of 7fiz by Molmil](/molmil-images/mine/7fiz) | Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex (conformation 3) | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, Lon protease, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... | Authors: | Li, S, Hsieh, K, Kuo, C, Su, S, Huang, K, Zhang, K, Chang, C.I. | Deposit date: | 2021-08-01 | Release date: | 2021-11-24 | Last modified: | 2024-06-12 | Method: | ELECTRON MICROSCOPY (3.28 Å) | Cite: | Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex. Sci Adv, 7, 2021
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7FIE
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![BU of 7fie by Molmil](/molmil-images/mine/7fie) | Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex (conformation 2) | Descriptor: | ADENOSINE-5'-DIPHOSPHATE, Lon protease, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... | Authors: | Li, S, Hsieh, K, Kuo, C, Su, S, Huang, K, Zhang, K, Chang, C.I. | Deposit date: | 2021-07-31 | Release date: | 2021-11-24 | Last modified: | 2024-06-12 | Method: | ELECTRON MICROSCOPY (2.36 Å) | Cite: | Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex. Sci Adv, 7, 2021
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7EUY
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![BU of 7euy by Molmil](/molmil-images/mine/7euy) | Crystal structure of the Lon-like protease MtaLonC with D582A mutation in complex with substrate polypeptide | Descriptor: | ALA-PRO-GLU-ALA-VAL, Endopeptidase La, PHOSPHATE ION | Authors: | Hsieh, K.Y, Kuo, C.I, Su, S.C, Huang, K.F, Chang, C.I. | Deposit date: | 2021-05-19 | Release date: | 2021-11-24 | Last modified: | 2023-11-29 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex. Sci Adv, 7, 2021
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7EV6
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![BU of 7ev6 by Molmil](/molmil-images/mine/7ev6) | Crystal structure of the Lon-like protease MtaLonC with D581A mutation in complex with F-b20-Q | Descriptor: | Endopeptidase La, F-b20-Q peptide {ortho-aminobenzoic acid (Abz)- QLRSLNGEWRFAWFPAPEAV[Tyr(3-NO2)]A}, PHOSPHATE ION | Authors: | Hsieh, K.Y, Kuo, C.I, Su, S.C, Huang, K.F, Chang, C.I. | Deposit date: | 2021-05-20 | Release date: | 2021-11-24 | Last modified: | 2023-11-29 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex. Sci Adv, 7, 2021
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7EUX
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![BU of 7eux by Molmil](/molmil-images/mine/7eux) | Crystal structure of the Lon-like protease MtaLonC with D581A mutation in complex with substrate polypeptide | Descriptor: | ALA-PRO-GLU-ALA-VAL, Endopeptidase La, PHOSPHATE ION | Authors: | Hsieh, K.Y, Kuo, C.I, Su, S.C, Huang, K.F, Chang, C.I. | Deposit date: | 2021-05-19 | Release date: | 2021-11-24 | Last modified: | 2023-11-29 | Method: | X-RAY DIFFRACTION (2.25 Å) | Cite: | Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex. Sci Adv, 7, 2021
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