8BBX
 
 | | Structure of prolyl endoprotease from Aspergillus niger CBS 109712 in space group C222(1) | | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, Endoprotease endo-Pro, TETRAETHYLENE GLYCOL, ... | | 著者 | Pijning, T, Vujicic-Zagar, A, Van der Laan, J.M, De Jong, R.M, Dijkstra, B.W. | | 登録日 | 2022-10-14 | | 公開日 | 2023-12-20 | | 最終更新日 | 2024-10-23 | | 実験手法 | X-RAY DIFFRACTION (2.7 Å) | | 主引用文献 | Structural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger.
Protein Sci., 33, 2024
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8B57
 | | Structure of prolyl endoprotease from Aspergillus niger CBS 109712 | | 分子名称: | 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, DI(HYDROXYETHYL)ETHER, ... | | 著者 | Pijning, T, Vujicic-Zagar, A, Van der Laan, J.M, De Jong, R.M, Dijkstra, B.W. | | 登録日 | 2022-09-22 | | 公開日 | 2023-12-20 | | 最終更新日 | 2024-01-10 | | 実験手法 | X-RAY DIFFRACTION (2.42 Å) | | 主引用文献 | Structural and time-resolved mechanistic investigations of protein hydrolysis by the acidic proline-specific endoprotease from Aspergillus niger.
Protein Sci., 33, 2024
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1FXH
 | | MUTANT OF PENICILLIN ACYLASE IMPAIRED IN CATALYSIS WITH PHENYLACETIC ACID IN THE ACTIVE SITE | | 分子名称: | 2-PHENYLACETIC ACID, CALCIUM ION, PENICILLIN ACYLASE | | 著者 | Alkema, W.B, Hensgens, C.M, Kroezinga, E.H, de Vries, E, Floris, R, van der Laan, J.M, Dijkstra, B.W, Janssen, D.B. | | 登録日 | 2000-09-26 | | 公開日 | 2001-03-28 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (1.97 Å) | | 主引用文献 | Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies.
Protein Eng., 13, 2000
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1FXV
 | | PENICILLIN ACYLASE MUTANT IMPAIRED IN CATALYSIS WITH PENICILLIN G IN THE ACTIVE SITE | | 分子名称: | CALCIUM ION, PENICILLIN ACYLASE, PENICILLIN G | | 著者 | Alkema, W.B, Hensgens, C.M, Kroezinga, E.H, de Vries, E, Floris, R, van der Laan, J.M, Dijkstra, B.W, Janssen, D.B. | | 登録日 | 2000-09-27 | | 公開日 | 2001-03-28 | | 最終更新日 | 2024-02-07 | | 実験手法 | X-RAY DIFFRACTION (2.25 Å) | | 主引用文献 | Characterization of the beta-lactam binding site of penicillin acylase of Escherichia coli by structural and site-directed mutagenesis studies.
Protein Eng., 13, 2000
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2X1D
 | | The crystal structure of mature acyl coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum | | 分子名称: | (4S,5S)-1,2-DITHIANE-4,5-DIOL, ACETATE ION, ACYL-COENZYME, ... | | 著者 | Bokhove, M, Yoshida, H, Hensgens, C.M.H, van der Laan, J.M, Sutherland, J.D, Dijkstra, B.W. | | 登録日 | 2009-12-23 | | 公開日 | 2010-03-09 | | 最終更新日 | 2024-10-23 | | 実験手法 | X-RAY DIFFRACTION (1.64 Å) | | 主引用文献 | Structures of an Isopenicillin N Converting Ntn-Hydrolase Reveal Different Catalytic Roles for the Active Site Residues of Precursor and Mature Enzyme.
Structure, 18, 2010
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2X1C
 | | The crystal structure of precursor acyl coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum | | 分子名称: | ACYL-COENZYME, CHLORIDE ION, GLYCEROL, ... | | 著者 | Bokhove, M, Yoshida, H, Hensgens, C.M.H, van der Laan, J.M, Sutherland, J.D, Dijkstra, B.W. | | 登録日 | 2009-12-23 | | 公開日 | 2010-03-09 | | 最終更新日 | 2024-05-08 | | 実験手法 | X-RAY DIFFRACTION (1.85 Å) | | 主引用文献 | Structures of an Isopenicillin N Converting Ntn-Hydrolase Reveal Different Catalytic Roles for the Active Site Residues of Precursor and Mature Enzyme.
Structure, 18, 2010
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2X1E
 | | The crystal structure of mature acyl coenzyme A:isopenicillin N acyltransferase from Penicillium chrysogenum in complex 6- aminopenicillanic acid | | 分子名称: | (2S,5R,6R)-6-AMINO-3,3-DIMETHYL-7-OXO-4-THIA-1-AZABICYCLO[3.2.0]HEPTANE-2-CARBOXYLIC ACID, ACYL-COENZYME, CHLORIDE ION, ... | | 著者 | Bokhove, M, Yoshida, H, Hensgens, C.M.H, van der Laan, J.M, Sutherland, J.D, Dijkstra, B.W. | | 登録日 | 2009-12-23 | | 公開日 | 2010-03-09 | | 最終更新日 | 2023-12-20 | | 実験手法 | X-RAY DIFFRACTION (2 Å) | | 主引用文献 | Structures of an Isopenicillin N Converting Ntn-Hydrolase Reveal Different Catalytic Roles for the Active Site Residues of Precursor and Mature Enzyme.
Structure, 18, 2010
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