1ISB
| STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS | Descriptor: | FE (III) ION, IRON(III) SUPEROXIDE DISMUTASE | Authors: | Lah, M.S, Dixon, M, Pattridge, K.A, Stallings, W.C, Fee, J.A, Ludwig, M.L. | Deposit date: | 1994-07-12 | Release date: | 1994-09-30 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.85 Å) | Cite: | Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry, 34, 1995
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1ISA
| STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS | Descriptor: | FE (II) ION, IRON(II) SUPEROXIDE DISMUTASE | Authors: | Lah, M.S, Dixon, M, Pattridge, K.A, Stallings, W.C, Fee, J.A, Ludwig, M.L. | Deposit date: | 1994-07-12 | Release date: | 1994-09-30 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry, 34, 1995
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1ISC
| STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS | Descriptor: | AZIDE ION, FE (III) ION, IRON(III) SUPEROXIDE DISMUTASE | Authors: | Lah, M.S, Dixon, M, Pattridge, K.A, Stallings, W.C, Fee, J.A, Ludwig, M.L. | Deposit date: | 1994-07-12 | Release date: | 1994-09-30 | Last modified: | 2024-02-07 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry, 34, 1995
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1MNG
| STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE: COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS | Descriptor: | AZIDE ION, MANGANESE (II) ION, MANGANESE SUPEROXIDE DISMUTASE | Authors: | Lah, M.S, Dixon, M, Pattridge, K.A, Stallings, W.C, Fee, J.A, Ludwig, M.L. | Deposit date: | 1994-07-13 | Release date: | 1994-10-15 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (1.8 Å) | Cite: | Structure-function in Escherichia coli iron superoxide dismutase: comparisons with the manganese enzyme from Thermus thermophilus. Biochemistry, 34, 1995
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1PXA
| CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS | Descriptor: | FLAVIN-ADENINE DINUCLEOTIDE, P-HYDROXYBENZOATE HYDROXYLASE, P-HYDROXYBENZOIC ACID | Authors: | Lah, M.S, Palfey, B.A, Schreuder, H.A, Ludwig, M.L. | Deposit date: | 1994-09-27 | Release date: | 1995-02-27 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants. Biochemistry, 33, 1994
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1PXB
| CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS | Descriptor: | FLAVIN-ADENINE DINUCLEOTIDE, P-HYDROXYBENZOATE HYDROXYLASE, P-HYDROXYBENZOIC ACID | Authors: | Lah, M.S, Palfey, B.A, Schreuder, H.A, Ludwig, M.L. | Deposit date: | 1994-09-27 | Release date: | 1995-02-27 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants. Biochemistry, 33, 1994
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1PXC
| CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS | Descriptor: | FLAVIN-ADENINE DINUCLEOTIDE, P-HYDROXYBENZOATE HYDROXYLASE, P-HYDROXYBENZOIC ACID | Authors: | Lah, M.S, Palfey, B.A, Schreuder, H.A, Ludwig, M.L. | Deposit date: | 1994-09-27 | Release date: | 1995-02-27 | Last modified: | 2024-02-14 | Method: | X-RAY DIFFRACTION (2.1 Å) | Cite: | Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants. Biochemistry, 33, 1994
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3RK4
| Structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant DhaA31 | Descriptor: | CHLORIDE ION, Haloalkane dehalogenase | Authors: | Lahoda, M, Stsiapanava, A, Mesters, J, Chaloupkova, R, Damborsky, J, Kuta Smatanova, I. | Deposit date: | 2011-04-17 | Release date: | 2012-04-18 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (1.31 Å) | Cite: | Crystallographic analysis of 1,2,3-trichloropropane biodegradation by the haloalkane dehalogenase DhaA31. Acta Crystallogr.,Sect.D, 70, 2014
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8C8A
| The NMR structure of the MAX28 effector from Magnaporthe oryzae | Descriptor: | But2 domain-containing protein | Authors: | Lahfa, M, Padilla, A, de Guillen, K, Kroj, T, Roumestand, C, Barthe, P. | Deposit date: | 2023-01-19 | Release date: | 2024-02-14 | Last modified: | 2024-09-04 | Method: | SOLUTION NMR | Cite: | The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. Plos Pathog., 20, 2024
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2VEK
| Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties | Descriptor: | 3-(BUTYLSULPHONYL)-PROPANOIC ACID, CITRIC ACID, TERTIARY-BUTYL ALCOHOL, ... | Authors: | Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-10-24 | Release date: | 2008-02-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.6 Å) | Cite: | Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties. Protein Eng.Des.Sel., 21, 2008
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2VEN
| Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties | Descriptor: | CITRIC ACID, GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE | Authors: | Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-10-25 | Release date: | 2008-02-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2 Å) | Cite: | Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties. Protein Eng.Des.Sel., 21, 2008
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2VEI
| Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties | Descriptor: | GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE, SULFATE ION | Authors: | Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-10-24 | Release date: | 2008-02-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (1.89 Å) | Cite: | Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties. Protein Eng.Des.Sel., 21, 2008
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2VEL
| Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties. | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, CHLORIDE ION, GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE | Authors: | Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-10-24 | Release date: | 2008-02-19 | Last modified: | 2024-05-01 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties. Protein Eng.Des.Sel., 21, 2008
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2VEM
| Structure-based enzyme engineering efforts with an inactive monomeric TIM variant: the importance of a single point mutation for generating an active site with suitable binding properties | Descriptor: | (3-bromo-2-oxo-propoxy)phosphonic acid, GLYCOSOMAL TRIOSEPHOSPHATE ISOMERASE, TERTIARY-BUTYL ALCOHOL | Authors: | Alahuhta, M, Salin, M, Casteleijn, M.G, Kemmer, C, El-Sayed, I, Augustyns, K, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-10-25 | Release date: | 2008-02-19 | Last modified: | 2024-10-16 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Structure-Based Protein Engineering Efforts with a Monomeric Tim Variant: The Importance of a Single Point Mutation for Generating an Active Site with Suitable Binding Properties. Protein Eng.Des.Sel., 21, 2008
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7ZJY
| The NMR structure of the MAX67 effector from Magnaporthe Oryzae | Descriptor: | MAX effector protein | Authors: | Lahfa, M, Padilla, A, de Guillen, K, Pissarra, J, Raji, M, Cesari, S, Kroj, T, Gladieux, P, Roumestand, C, Barthe, P. | Deposit date: | 2022-04-12 | Release date: | 2023-04-26 | Last modified: | 2024-10-23 | Method: | SOLUTION NMR | Cite: | The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. Plos Pathog., 20, 2024
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7ZK0
| The NMR structure of the MAX60 effector from Magnaporthe Oryzae | Descriptor: | MAX effector protein | Authors: | Lahfa, M, Padilla, A, de Guillen, K, Pissarra, J, Raji, M, Cesari, S, Kroj, T, Gladieux, P, Roumestand, C, Barthe, P. | Deposit date: | 2022-04-12 | Release date: | 2023-04-26 | Last modified: | 2024-09-04 | Method: | SOLUTION NMR | Cite: | The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. Plos Pathog., 20, 2024
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7ZKD
| The NMR structure of the MAX47 effector from Magnaporthe Oryzae | Descriptor: | MAX effector protein | Authors: | Lahfa, M, Padilla, A, de Guillen, K, Pissarra, J, Raji, M, Cesari, S, Kroj, T, Gladieux, P, Roumestand, C, Barthe, P. | Deposit date: | 2022-04-12 | Release date: | 2023-04-26 | Last modified: | 2024-11-06 | Method: | SOLUTION NMR | Cite: | The structural landscape and diversity of Pyricularia oryzae MAX effectors revisited. Plos Pathog., 20, 2024
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2V0T
| The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM | Descriptor: | 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | Authors: | Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-05-18 | Release date: | 2008-02-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.2 Å) | Cite: | Structural studies show that the A178L mutation in the C-terminal hinge of the catalytic loop-6 of triosephosphate isomerase (TIM) induces a closed-like conformation in dimeric and monomeric TIM. Acta Crystallogr. D Biol. Crystallogr., 64, 2008
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2V2H
| The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, CHLORIDE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | Authors: | Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-06-06 | Release date: | 2008-02-19 | Last modified: | 2024-05-01 | Method: | X-RAY DIFFRACTION (1.18 Å) | Cite: | Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed-Like Conformation in Dimeric and Monomeric Tim. Acta Crystallogr.,Sect.D, 64, 2008
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2V2D
| The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM | Descriptor: | PHOSPHATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | Authors: | Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-06-05 | Release date: | 2008-02-19 | Last modified: | 2023-12-13 | Method: | X-RAY DIFFRACTION (2.3 Å) | Cite: | Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed- Like Conformation in Dimeric and Monomeric Tim. Acta Crystallogr.,Sect.D, 64, 2008
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2V2C
| The A178L mutation in the C-terminal hinge of the flexible loop-6 of triosephosphate isomerase (TIM) induces a more closed conformation of this hinge region in dimeric and monomeric TIM | Descriptor: | 2-PHOSPHOGLYCOLIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL | Authors: | Alahuhta, M, Casteleijn, M.G, Neubauer, P, Wierenga, R.K. | Deposit date: | 2007-06-05 | Release date: | 2008-02-19 | Last modified: | 2024-05-01 | Method: | X-RAY DIFFRACTION (1.89 Å) | Cite: | Structural Studies Show that the A178L Mutation in the C-Terminal Hinge of the Catalytic Loop-6 of Triosephosphate Isomerase (Tim) Induces a Closed-Like Conformation in Dimeric and Monomeric Tim. Acta Crystallogr.,Sect.D, 64, 2008
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3SK0
| structure of Rhodococcus rhodochrous haloalkane dehalogenase DhaA mutant DhaA12 | Descriptor: | CHLORIDE ION, Haloalkane dehalogenase | Authors: | Lahoda, M, Stsiapanava, A, Mesters, J, Koudelakova, T, Damborsky, J, Kuta-Smatanova, I. | Deposit date: | 2011-06-22 | Release date: | 2012-06-27 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (1.78 Å) | Cite: | Dynamics and hydration explain failed functional transformation in dehalogenase design. Nat.Chem.Biol., 10, 2014
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4A0Q
| Activated Conformation of Integrin alpha1 I-Domain mutant | Descriptor: | INTEGRIN ALPHA-1, MAGNESIUM ION | Authors: | Lahti, M, Bligt, E, Niskanen, H, Parkash, V, Brandt, A.-M, Jokinen, J, Patrikainen, P, Kapyla, J, Heino, J, Salminen, T.A. | Deposit date: | 2011-09-12 | Release date: | 2011-10-26 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Structure of Collagen Receptor Integrin Aplha1I Domain Carrying the Activating Mutation E317A. J.Biol.Chem., 286, 2011
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3VTT
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4FWB
| Structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant DhaA31 in complex with 1, 2, 3 - trichloropropane | Descriptor: | 1,2,3-trichloropropane, CHLORIDE ION, Haloalkane dehalogenase | Authors: | Lahoda, M, Stsiapanava, A, Mesters, J, Kuta Smatanova, I. | Deposit date: | 2012-06-30 | Release date: | 2012-09-05 | Last modified: | 2023-09-13 | Method: | X-RAY DIFFRACTION (1.26 Å) | Cite: | Crystallographic analysis of 1,2,3-trichloropropane biodegradation by the haloalkane dehalogenase DhaA31. Acta Crystallogr.,Sect.D, 70, 2014
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