1E2L
 
 | | Kinetics and crystal structure of the wild-type and the engineered Y101F mutant of Herpes simplex virus type 1 thymidine kinase interacting with (North)-methanocarba-thymidine | | Descriptor: | 1-[4-HYDROXY-5-(HYDROXYMETHYL)BICYCLO[3.1.0]HEX-2-YL]-5-METHYLPYRIMIDINE-2,4(1H,3H)-DIONE, SULFATE ION, THYMIDINE KINASE | | Authors: | Vogt, J, Scapozza, L, Schulz, G.E. | | Deposit date: | 2000-05-23 | | Release date: | 2000-08-18 | | Last modified: | 2023-12-06 | | Method: | X-RAY DIFFRACTION (2.4 Å) | | Cite: | Kinetics and Crystal Structure of the Wild-Type and the Engineered Y101F Mutant of Herpes Simplex Virus Type 1 Thymidine Kinase Interacting with (North)-Methanocarba-Thymidine
Biochemistry, 39, 2000
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1GKJ
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1H7E
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1GT7
 | | L-rhamnulose-1-phosphate aldolase from Escherichia coli | | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, RHAMNULOSE-1-PHOSPHATE ALDOLASE, ZINC ION | | Authors: | Kroemer, M, Schulz, G.E. | | Deposit date: | 2002-01-14 | | Release date: | 2002-05-03 | | Last modified: | 2019-07-24 | | Method: | X-RAY DIFFRACTION (2.7 Å) | | Cite: | The Structure of L-Rhamnulose-1-Phosphate Aldolase (Class II) Solved by Low-Resolution Sir Phasing and 20-Fold Ncs Averaging
Acta Crystallogr.,Sect.D, 58, 2002
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1H7H
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1NKS
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1O9G
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1O9H
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1OG4
 | | Crystal Structure of the Eucaryotic Mono-ADP-Ribosyltransferase ART2.2 Mutant E189A in Complex with NADH | | Descriptor: | 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, T-CELL ECTO-ADP-RIBOSYLTRANSFERASE 2 | | Authors: | Ritter, H, Koch-Nolte, F, Marquez, V.E, Schulz, G.E. | | Deposit date: | 2003-04-24 | | Release date: | 2003-08-28 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.6 Å) | | Cite: | Substrate Binding and Catalysis of Ecto-Adp-Ribosyltransferase 2.2 From Rat
Biochemistry, 42, 2003
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1OG3
 | | Crystal structure of the eukaryotic mono-ADP-ribosyltransferase ART2.2 mutant E189I in complex with NAD | | Descriptor: | NICOTINAMIDE-ADENINE-DINUCLEOTIDE, T-CELL ECTO-ADP-RIBOSYLTRANSFERASE 2 | | Authors: | Ritter, H, Koch-Nolte, F, Marquez, V.E, Schulz, G.E. | | Deposit date: | 2003-04-24 | | Release date: | 2003-08-28 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.6 Å) | | Cite: | Substrate Binding and Catalysis of Ecto-Adp-Ribosyltransferase 2.2 From Rat
Biochemistry, 42, 2003
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1OKX
 | | Binding Structure of Elastase Inhibitor Scyptolin A | | Descriptor: | ELASTASE 1, SCYPTOLIN A | | Authors: | Matern, U, Schleberger, C, Jelakovic, S, Weckesser, J, Schulz, G.E. | | Deposit date: | 2003-07-31 | | Release date: | 2003-10-24 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2.8 Å) | | Cite: | Binding Structure of Elastase Inhibitor Scyptolin A
Chem.Biol., 10, 2003
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1OG1
 | | CRYSTAL STRUCTURE OF THE EUCARYOTIC MONO-ADP-RIBOSYLTRANSFERASE ART2.2 IN COMPLEX WITH TAD | | Descriptor: | BETA-METHYLENE-THIAZOLE-4-CARBOXYAMIDE-ADENINE DINUCLEOTIDE, T-CELL ECTO-ADP-RIBOSYLTRANSFERASE 2 | | Authors: | Ritter, H, Koch-Nolte, F, Marquez, V.E, Schulz, G.E. | | Deposit date: | 2003-04-23 | | Release date: | 2003-08-28 | | Last modified: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Substrate Binding and Catalysis of Ecto-Adp-Ribosyltransferase 2.2 From Rat
Biochemistry, 42, 2003
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1PBG
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1RPX
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1GER
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1FUI
 | | L-FUCOSE ISOMERASE FROM ESCHERICHIA COLI | | Descriptor: | FUCITOL, L-FUCOSE ISOMERASE, MANGANESE (II) ION, ... | | Authors: | Seemann, J.E, Schulz, G.E. | | Deposit date: | 1997-04-14 | | Release date: | 1997-10-15 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Structure and mechanism of L-fucose isomerase from Escherichia coli.
J.Mol.Biol., 273, 1997
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1GXY
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1H1Y
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1H1Z
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1GY0
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5PRN
 | | E1M, Y96W, S119W MUTANT OF RH. BLASTICA PORIN | | Descriptor: | (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, PORIN | | Authors: | Maveyraud, L, Schmid, B, Schulz, G.E. | | Deposit date: | 1998-06-12 | | Release date: | 1998-08-12 | | Last modified: | 2023-08-09 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Porin mutants with new channel properties.
Protein Sci., 7, 1998
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5GRT
 | | HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, GLUTATHIONYLSPERMIDINE COMPLEX | | Descriptor: | FLAVIN-ADENINE DINUCLEOTIDE, GLUTATHIONE REDUCTASE, GLUTATHIONYLSPERMIDINE DISULFIDE | | Authors: | Stoll, V.S, Simpson, S.J, Krauth-Siegel, R.L, Walsh, C.T, Pai, E.F. | | Deposit date: | 1997-02-12 | | Release date: | 1997-08-12 | | Last modified: | 2023-08-09 | | Method: | X-RAY DIFFRACTION (2.4 Å) | | Cite: | Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
Biochemistry, 36, 1997
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4GRT
 | | HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, MIXED DISULFIDE BETWEEN TRYPANOTHIONE AND THE ENZYME | | Descriptor: | BIS(GAMMA-GLUTAMYL-CYSTEINYL-GLYCINYL)SPERMIDINE, FLAVIN-ADENINE DINUCLEOTIDE, GLUTATHIONE REDUCTASE | | Authors: | Stoll, V.S, Simpson, S.J, Krauth-Siegel, R.L, Walsh, C.T, Pai, E.F. | | Deposit date: | 1997-02-12 | | Release date: | 1997-08-12 | | Last modified: | 2023-08-09 | | Method: | X-RAY DIFFRACTION (2.8 Å) | | Cite: | Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
Biochemistry, 36, 1997
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1GRT
 | | HUMAN GLUTATHIONE REDUCTASE A34E/R37W MUTANT | | Descriptor: | FLAVIN-ADENINE DINUCLEOTIDE, GLUTATHIONE REDUCTASE | | Authors: | Stoll, V.S, Simpson, S.J, Krauth-Siegel, R.L, Walsh, C.T, Pai, E.F. | | Deposit date: | 1996-12-17 | | Release date: | 1997-06-16 | | Last modified: | 2023-08-09 | | Method: | X-RAY DIFFRACTION (2.3 Å) | | Cite: | Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
Biochemistry, 36, 1997
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3GRT
 | | HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED TRYPANOTHIONE COMPLEX | | Descriptor: | 2-AMINO-4-[4-(4-AMINO-4-CARBOXY-BUTYRYLAMINO)-5,8,19,22-TETRAOXO-1,2-DITHIA-6,9,13,18,21-PENTAAZA-CYCLOTETRACOS-23-YLCARBAMOYL]-BUTYRIC ACID, FLAVIN-ADENINE DINUCLEOTIDE, GLUTATHIONE REDUCTASE | | Authors: | Stoll, V.S, Simpson, S.J, Krauth-Siegel, R.L, Walsh, C.T, Pai, E.F. | | Deposit date: | 1997-02-12 | | Release date: | 1997-08-12 | | Last modified: | 2023-08-09 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
Biochemistry, 36, 1997
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