3KG1
 
 | | Crystal structure of SnoaB, a cofactor-independent oxygenase from Streptomyces nogalater, mutant N63A | | Descriptor: | CHLORIDE ION, SnoaB | | Authors: | Koskiniemi, H, Grocholski, T, Lindqvist, Y, Mantsala, P, Niemi, J, Schneider, G. | | Deposit date: | 2009-10-28 | | Release date: | 2010-01-26 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Crystal structure of the cofactor-independent monooxygenase SnoaB from Streptomyces nogalater: implications for the reaction mechanism
Biochemistry, 49, 2010
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3KG0
 | | Crystal structure of SnoaB, a cofactor-independent oxygenase from Streptomyces nogalater, determined to 1.7 resolution | | Descriptor: | 1,2-ETHANEDIOL, CHLORIDE ION, SnoaB | | Authors: | Koskiniemi, H, Grocholski, T, Lindqvist, Y, Mantsala, P, Niemi, J, Schneider, G. | | Deposit date: | 2009-10-28 | | Release date: | 2010-01-26 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (1.7 Å) | | Cite: | Crystal structure of the cofactor-independent monooxygenase SnoaB from Streptomyces nogalater: implications for the reaction mechanism
Biochemistry, 49, 2010
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3KNG
 | | Crystal structure of SnoaB, a cofactor-independent oxygenase from Streptomyces nogalater, determined to 1.9 resolution | | Descriptor: | 1,2-ETHANEDIOL, CHLORIDE ION, SULFATE ION, ... | | Authors: | Koskiniemi, H, Grocholski, T, Lindqvist, Y, Mantsala, P, Niemi, J, Schneider, G. | | Deposit date: | 2009-11-12 | | Release date: | 2010-01-26 | | Last modified: | 2023-09-06 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | Crystal structure of the cofactor-independent monooxygenase SnoaB from Streptomyces nogalater: implications for the reaction mechanism
Biochemistry, 49, 2010
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2QA1
 | | Crystal structure of PgaE, an aromatic hydroxylase involved in angucycline biosynthesis | | Descriptor: | 1,2-ETHANEDIOL, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... | | Authors: | Koskiniemi, H, Dobritzsch, D, Metsa-Ketela, M, Kallio, P, Niemi, J, Schneider, G. | | Deposit date: | 2007-06-14 | | Release date: | 2007-08-14 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (1.8 Å) | | Cite: | Crystal structures of two aromatic hydroxylases involved in the early tailoring steps of angucycline biosynthesis
J.Mol.Biol., 372, 2007
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2QA2
 | | Crystal structure of CabE, an aromatic hydroxylase from angucycline biosynthesis, determined to 2.7 A resolution | | Descriptor: | FLAVIN-ADENINE DINUCLEOTIDE, Polyketide oxygenase CabE | | Authors: | Koskiniemi, H, Dobritzsch, D, Metsa-Ketela, M, Kallio, P, Niemi, J, Schneider, G. | | Deposit date: | 2007-06-14 | | Release date: | 2007-08-14 | | Last modified: | 2023-08-30 | | Method: | X-RAY DIFFRACTION (2.7 Å) | | Cite: | Crystal structures of two aromatic hydroxylases involved in the early tailoring steps of angucycline biosynthesis
J.Mol.Biol., 372, 2007
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3IHG
 | | Crystal structure of a ternary complex of aklavinone-11 hydroxylase with FAD and aklavinone | | Descriptor: | FLAVIN-ADENINE DINUCLEOTIDE, RdmE, SULFATE ION, ... | | Authors: | Lindqvist, Y, Koskiniemi, H, Jansson, A, Sandalova, T, Schneider, G. | | Deposit date: | 2009-07-30 | | Release date: | 2009-09-29 | | Last modified: | 2024-02-21 | | Method: | X-RAY DIFFRACTION (2.49 Å) | | Cite: | Structural basis for substrate recognition and specificity in aklavinone-11-hydroxylase from rhodomycin biosynthesis.
J.Mol.Biol., 393, 2009
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1XDS
 | | Crystal structure of Aclacinomycin-10-hydroxylase (RdmB) in complex with S-adenosyl-L-methionine (SAM) and 11-deoxy-beta-rhodomycin (DbrA) | | Descriptor: | 11-DEOXY-BETA-RHODOMYCIN, Protein RdmB, S-ADENOSYLMETHIONINE | | Authors: | Jansson, A, Koskiniemi, H, Erola, A, Wang, J, Mantsala, P, Schneider, G, Niemi, J, Structural Proteomics in Europe (SPINE) | | Deposit date: | 2004-09-08 | | Release date: | 2004-11-23 | | Last modified: | 2024-10-30 | | Method: | X-RAY DIFFRACTION (2.3 Å) | | Cite: | Aclacinomycin 10-Hydroxylase Is a Novel Substrate-assisted Hydroxylase Requiring S-Adenosyl-L-methionine as Cofactor
J.Biol.Chem., 280, 2005
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1TW3
 | | Crystal structure of Carminomycin-4-O-methyltransferase (DnrK) in complex with S-adenosyl-L-homocystein (SAH) and 4-methoxy-e-rhodomycin T (M-ET) | | Descriptor: | Carminomycin 4-O-methyltransferase, METHYL (4R)-2-ETHYL-2,5,12-TRIHYDROXY-7-METHOXY-6,11-DIOXO-4-{[2,3,6-TRIDEOXY-3-(DIMETHYLAMINO)-BETA-D-RIBO-HEXOPYRANOSYL]OXY}-1H,2H,3H,4H,6H,11H-TETRACENE-1-CARBOXYLATE, S-ADENOSYL-L-HOMOCYSTEINE | | Authors: | Jansson, A, Koskiniemi, H, Mantsala, P, Niemi, J, Schneider, G. | | Deposit date: | 2004-06-30 | | Release date: | 2004-09-14 | | Last modified: | 2024-04-03 | | Method: | X-RAY DIFFRACTION (2.35 Å) | | Cite: | Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products
J.Biol.Chem., 279, 2004
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1XDU
 | | Crystal structure of Aclacinomycin-10-hydroxylase (RdmB) in complex with Sinefungin (SFG) | | Descriptor: | ACETATE ION, Protein RdmB, SINEFUNGIN | | Authors: | Jansson, A, Koskiniemi, H, Erola, A, Wang, J, Mantsala, P, Schneider, G, Niemi, J. | | Deposit date: | 2004-09-08 | | Release date: | 2004-11-23 | | Last modified: | 2024-11-06 | | Method: | X-RAY DIFFRACTION (2.7 Å) | | Cite: | Aclacinomycin 10-Hydroxylase Is a Novel Substrate-assisted Hydroxylase Requiring S-Adenosyl-L-methionine as Cofactor
J.Biol.Chem., 280, 2005
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1TW2
 | | Crystal structure of Carminomycin-4-O-methyltransferase (DnrK) in complex with S-adenosyl-L-homocystein (SAH) and 4-methoxy-e-rhodomycin T (M-ET) | | Descriptor: | Carminomycin 4-O-methyltransferase, METHYL (4R)-2-ETHYL-2,5,12-TRIHYDROXY-7-METHOXY-6,11-DIOXO-4-{[2,3,6-TRIDEOXY-3-(DIMETHYLAMINO)-BETA-D-RIBO-HEXOPYRANOSYL]OXY}-1H,2H,3H,4H,6H,11H-TETRACENE-1-CARBOXYLATE, S-ADENOSYL-L-HOMOCYSTEINE | | Authors: | Jansson, A, Koskiniemi, H, Mantsala, P, Niemi, J, Schneider, G, Structural Proteomics in Europe (SPINE) | | Deposit date: | 2004-06-30 | | Release date: | 2004-09-14 | | Last modified: | 2024-04-03 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Crystal structure of a ternary complex of DnrK, a methyltransferase in daunorubicin biosynthesis, with bound products
J.Biol.Chem., 279, 2004
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