7AZ9
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![BU of 7az9 by Molmil](/molmil-images/mine/7az9) | Perdeuterated E65Q-TIM complexed with PHOSPHOGLYCOLOHYDROXAMATE | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, Triosephosphate isomerase | Authors: | Kelpsas, V, Caldararu, O, von Wachenfeldt, C, Oksanen, E. | Deposit date: | 2020-11-16 | Release date: | 2021-07-28 | Last modified: | 2024-05-01 | Method: | NEUTRON DIFFRACTION (1.1 Å), X-RAY DIFFRACTION | Cite: | Neutron structures of Leishmania mexicana triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps. Iucrj, 8, 2021
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7AZA
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![BU of 7aza by Molmil](/molmil-images/mine/7aza) | Perdeuterated E65Q-TIM complexed with PHOSPHOGLYCOLOHYDROXAMATE | Descriptor: | PHOSPHOGLYCOLOHYDROXAMIC ACID, Triosephosphate isomerase | Authors: | Kelpsas, V, Caldararu, O, von Wachenfeldt, C, Oksanen, E. | Deposit date: | 2020-11-16 | Release date: | 2021-07-28 | Last modified: | 2024-05-01 | Method: | NEUTRON DIFFRACTION (1.1 Å), X-RAY DIFFRACTION | Cite: | Neutron structures of Leishmania mexicana triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps. Iucrj, 8, 2021
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7AZ4
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![BU of 7az4 by Molmil](/molmil-images/mine/7az4) | Perdeuterated E65Q-TIM complexed with 2-PHOSPHOGLYCOLIC ACID | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, Triosephosphate isomerase | Authors: | Kelpsas, V, Caldararu, O, von Wachenfeldt, C, Oksanen, E. | Deposit date: | 2020-11-16 | Release date: | 2021-07-28 | Last modified: | 2024-05-01 | Method: | NEUTRON DIFFRACTION (1.15 Å), X-RAY DIFFRACTION | Cite: | Neutron structures of Leishmania mexicana triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps. Iucrj, 8, 2021
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7AZ3
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![BU of 7az3 by Molmil](/molmil-images/mine/7az3) | Perdeuterated E65Q-TIM complexed with 2-PHOSPHOGLYCOLIC ACID | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, Triosephosphate isomerase | Authors: | Kelpsas, V, Caldararu, O, von Wachenfeldt, C, Oksanen, E. | Deposit date: | 2020-11-16 | Release date: | 2021-07-28 | Last modified: | 2024-05-01 | Method: | NEUTRON DIFFRACTION (1.15 Å), X-RAY DIFFRACTION | Cite: | Neutron structures of Leishmania mexicana triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps. Iucrj, 8, 2021
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1BKW
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![BU of 1bkw by Molmil](/molmil-images/mine/1bkw) | p-Hydroxybenzoate hydroxylase (phbh) mutant with cys116 replaced by ser (c116s) and arg44 replaced by lys (r44k), in complex with fad and 4-hydroxybenzoic acid | Descriptor: | FLAVIN-ADENINE DINUCLEOTIDE, P-HYDROXYBENZOIC ACID, PROTEIN (P-HYDROXYBENZOATE HYDROXYLASE) | Authors: | Eppink, M.H, Schreuder, H.A, Van Berkel, W.J. | Deposit date: | 1998-07-13 | Release date: | 1998-07-22 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding. Eur.J.Biochem., 231, 1995
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1CJ2
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![BU of 1cj2 by Molmil](/molmil-images/mine/1cj2) | MUTANT GLN34ARG OF PARA-HYDROXYBENZOATE HYDROXYLASE | Descriptor: | FLAVIN-ADENINE DINUCLEOTIDE, P-HYDROXYBENZOIC ACID, PROTEIN (P-HYDROXYBENZOATE HYDROXYLASE) | Authors: | Eppink, M.H.M, Overkamp, K.M, Schreuder, H.A, Van Berkel, W.J.H. | Deposit date: | 1999-04-21 | Release date: | 1999-04-30 | Last modified: | 2023-08-09 | Method: | X-RAY DIFFRACTION (2.8 Å) | Cite: | Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase. J.Mol.Biol., 292, 1999
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1AMK
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![BU of 1amk by Molmil](/molmil-images/mine/1amk) | LEISHMANIA MEXICANA TRIOSE PHOSPHATE ISOMERASE | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, TRIOSE PHOSPHATE ISOMERASE | Authors: | Williams, J.C, Wierenga, R. | Deposit date: | 1997-06-17 | Release date: | 1997-12-17 | Last modified: | 2024-05-22 | Method: | X-RAY DIFFRACTION (1.83 Å) | Cite: | Structural and mutagenesis studies of leishmania triosephosphate isomerase: a point mutation can convert a mesophilic enzyme into a superstable enzyme without losing catalytic power. Protein Eng., 12, 1999
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5I3F
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![BU of 5i3f by Molmil](/molmil-images/mine/5i3f) | Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase | Descriptor: | Triosephosphate isomerase, glycosomal | Authors: | Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J. | Deposit date: | 2016-02-10 | Release date: | 2016-05-18 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (1.72 Å) | Cite: | Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase. Biochemistry, 55, 2016
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5I3H
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![BU of 5i3h by Molmil](/molmil-images/mine/5i3h) | Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, POTASSIUM ION, Triosephosphate isomerase, ... | Authors: | Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J. | Deposit date: | 2016-02-10 | Release date: | 2016-05-18 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (2.25 Å) | Cite: | Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase. Biochemistry, 55, 2016
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5I3J
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![BU of 5i3j by Molmil](/molmil-images/mine/5i3j) | Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase | Descriptor: | SODIUM ION, Triosephosphate isomerase, glycosomal | Authors: | Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J. | Deposit date: | 2016-02-10 | Release date: | 2016-05-18 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase. Biochemistry, 55, 2016
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5I3I
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![BU of 5i3i by Molmil](/molmil-images/mine/5i3i) | Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, Triosephosphate isomerase, glycosomal | Authors: | Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J. | Deposit date: | 2016-02-10 | Release date: | 2016-05-18 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase. Biochemistry, 55, 2016
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5I3K
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![BU of 5i3k by Molmil](/molmil-images/mine/5i3k) | Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, SODIUM ION, Triosephosphate isomerase, ... | Authors: | Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J. | Deposit date: | 2016-02-10 | Release date: | 2016-05-18 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (2.209 Å) | Cite: | Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase. Biochemistry, 55, 2016
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5I3G
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![BU of 5i3g by Molmil](/molmil-images/mine/5i3g) | Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase | Descriptor: | Triosephosphate isomerase, glycosomal | Authors: | Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J. | Deposit date: | 2016-02-10 | Release date: | 2016-05-18 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (1.96 Å) | Cite: | Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase. Biochemistry, 55, 2016
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4GRT
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![BU of 4grt by Molmil](/molmil-images/mine/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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1H9G
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![BU of 1h9g by Molmil](/molmil-images/mine/1h9g) | FadR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI, in complex with myristoyl-CoA | Descriptor: | COENZYME A, FATTY ACID METABOLISM REGULATOR PROTEIN, MYRISTIC ACID | Authors: | Van Aalten, D.M.F, Dirusso, C.C, Knudsen, J. | Deposit date: | 2001-03-09 | Release date: | 2001-03-09 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | The Structural Basis of Acyl Coenzyme A-Dependent Regulation of the Transcription Factor Fadr Embo J., 20, 2001
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1H9T
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![BU of 1h9t by Molmil](/molmil-images/mine/1h9t) | FADR, FATTY ACID RESPONSIVE TRANSCRIPTION FACTOR FROM E. COLI IN COMPLEX WITH FADB OPERATOR | Descriptor: | 5'-D(*CP*AP*TP*CP*TP*GP*GP*TP*AP*CP*GP*AP* CP*CP*AP*GP*AP*TP*C)-3', 5'-D(*GP*AP*TP*CP*TP*GP*GP*TP*CP*GP*TP*AP* CP*CP*AP*GP*AP*TP*G)-3', CHLORIDE ION, ... | Authors: | Van Aalten, D.M.F, Dirusso, C.C, Knudsen, J. | Deposit date: | 2001-03-19 | Release date: | 2001-04-04 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (3.25 Å) | Cite: | The Structural Basis of Acyl Coenzyme A-Dependent Regulation of the Transcription Factor Fadr Embo J., 20, 2001
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1SHF
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![BU of 1shf by Molmil](/molmil-images/mine/1shf) | |
3LAD
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![BU of 3lad by Molmil](/molmil-images/mine/3lad) | |
1AG1
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![BU of 1ag1 by Molmil](/molmil-images/mine/1ag1) | |
1IKT
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![BU of 1ikt by Molmil](/molmil-images/mine/1ikt) | |
2X0N
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![BU of 2x0n by Molmil](/molmil-images/mine/2x0n) | Structure of glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei determined from Laue data | Descriptor: | GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, GLYCOSOMAL, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... | Authors: | Vellieux, F.M.D, Hajdu, J, Hol, W.G.J. | Deposit date: | 2009-12-16 | Release date: | 2009-12-22 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (3.2 Å) | Cite: | Structure of Glycosomal Glyceraldehyde-3-Phosphate Dehydrogenase from Trypanosoma Brucei Determined from Laue Data. Proc.Natl.Acad.Sci.USA, 90, 1993
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1SHG
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![BU of 1shg by Molmil](/molmil-images/mine/1shg) | CRYSTAL STRUCTURE OF A SRC-HOMOLOGY 3 (SH3) DOMAIN | Descriptor: | ALPHA-SPECTRIN SH3 DOMAIN | Authors: | Noble, M, Pauptit, R, Musacchio, A, Saraste, M, Wierenga, R.K. | Deposit date: | 1993-05-19 | Release date: | 1993-10-31 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Crystal structure of a Src-homology 3 (SH3) domain. Nature, 359, 1992
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3GRT
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![BU of 3grt by Molmil](/molmil-images/mine/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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3GRS
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![BU of 3grs by Molmil](/molmil-images/mine/3grs) | |
2PHI
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![BU of 2phi by Molmil](/molmil-images/mine/2phi) | A LARGE CONFORMATIONAL CHANGE IS FOUND IN THE CRYSTAL STRUCTURE OF THE PORCINE PANCREATIC PHOSPHOLIPASE A2 POINT MUTANT F63V | Descriptor: | CALCIUM ION, PHOSPHOLIPASE A2 | Authors: | Dijkstra, B.W, Thunnissen, M.M.G.M, Kalk, K.H, Drenth, J. | Deposit date: | 1993-04-08 | Release date: | 1993-07-15 | Last modified: | 2024-06-05 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Crystal structure of a porcine pancreatic phospholipase A2 mutant. A large conformational change caused by the F63V point mutation. J.Mol.Biol., 232, 1993
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