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2VU0
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BU of 2vu0 by Molmil
Biosynthetic thiolase from Z. ramigera. Complex of the oxidised enzyme with coenzyme A.
Descriptor: Acetyl-CoA acetyltransferase, COENZYME A, GLYCEROL, ...
Authors:Kursula, P, Wierenga, R.K.
Deposit date:2008-05-19
Release date:2008-10-28
Last modified:2019-07-24
Method:X-RAY DIFFRACTION (1.87 Å)
Cite:The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme.
FEBS J., 275, 2008
2VU2
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BU of 2vu2 by Molmil
Biosynthetic thiolase from Z. ramigera. Complex with S-pantetheine-11- pivalate.
Descriptor: (3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl 2,2-dimethylpropanoate, ACETYL-COA ACETYLTRANSFERASE, SULFATE ION
Authors:Kursula, P, Merilainen, G, Schmitz, W, Wierenga, R.K.
Deposit date:2008-05-19
Release date:2008-10-28
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.65 Å)
Cite:The Sulfur Atoms of the Substrate Coa and the Catalytic Cysteine are Required for a Productive Mode of Substrate Binding in Bacterial Biosynthetic Thiolase, a Thioester-Dependent Enzyme.
FEBS J., 275, 2008
2VXN
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BU of 2vxn by Molmil
E65Q-TIM complexed with phosphoglycolohydroxamate at 0.82 A resolution
Descriptor: 2-PHOSPHOGLYCOLIC ACID, ACETATE ION, GLYCEROL, ...
Authors:Alahuhta, M, Wierenga, R.K.
Deposit date:2008-07-08
Release date:2009-07-14
Last modified:2024-05-01
Method:X-RAY DIFFRACTION (0.82 Å)
Cite:Atomic Resolution Crystallography of a Complex of Triosephosphate Isomerase with a Reaction-Intermediate Analog: New Insight in the Proton Transfer Reaction Mechanism
Proteins, 78, 2010
2V2C
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BU of 2v2c by Molmil
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
2V2H
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BU of 2v2h by Molmil
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
2WKU
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BU of 2wku by Molmil
BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. THE N316H MUTANT.
Descriptor: ACETYL-COA ACETYLTRANSFERASE, D-mannose, SULFATE ION
Authors:Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K.
Deposit date:2009-06-18
Release date:2009-11-03
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Biochemistry, 48, 2009
2WL4
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BU of 2wl4 by Molmil
BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE H348A MUTANT WITH COENZYME A.
Descriptor: ACETYL-COA ACETYLTRANSFERASE, CHLORIDE ION, COENZYME A, ...
Authors:Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K.
Deposit date:2009-06-22
Release date:2009-11-03
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Biochemistry, 48, 2009
2WKT
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BU of 2wkt by Molmil
BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316A MUTANT WITH COENZYME A.
Descriptor: ACETYL-COA ACETYLTRANSFERASE, CHLORIDE ION, COENZYME A, ...
Authors:Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K.
Deposit date:2009-06-18
Release date:2009-11-03
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2 Å)
Cite:The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Biochemistry, 48, 2009
2WL6
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BU of 2wl6 by Molmil
BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. THE N316H-H348N MUTANT.
Descriptor: ACETYL-COA ACETYLTRANSFERASE
Authors:Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K.
Deposit date:2009-06-22
Release date:2009-11-03
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.98 Å)
Cite:The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Biochemistry, 48, 2009
2WL5
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BU of 2wl5 by Molmil
BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE H348N MUTANT WITH COENZYME A.
Descriptor: ACETYL-COA ACETYLTRANSFERASE, CHLORIDE ION, COENZYME A, ...
Authors:Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K.
Deposit date:2009-06-22
Release date:2009-11-03
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Biochemistry, 48, 2009
2WKV
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BU of 2wkv by Molmil
BIOSYNTHETIC THIOLASE FROM Z. RAMIGERA. COMPLEX OF THE N316D MUTANT WITH COENZYME A.
Descriptor: ACETYL-COA ACETYLTRANSFERASE, COENZYME A, SODIUM ION, ...
Authors:Merilainen, G, Poikela, V, Kursula, P, Wierenga, R.K.
Deposit date:2009-06-18
Release date:2009-11-03
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:The Thiolase Reaction Mechanism: The Importance of Asn316 and His348 for Stabilizing the Enolate Intermediate of the Claisen Condensation.
Biochemistry, 48, 2009
2VU1
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BU of 2vu1 by Molmil
Biosynthetic thiolase from Z. ramigera. Complex of with O-pantheteine- 11-pivalate.
Descriptor: ACETYL-COA ACETYLTRANSFERASE, PANTOTHENYL-AMINOETHANOL-11-PIVALIC ACID, SODIUM ION, ...
Authors:Kursula, P, Schmitz, W, Wierenga, R.K.
Deposit date:2008-05-19
Release date:2008-10-28
Last modified:2019-07-24
Method:X-RAY DIFFRACTION (1.51 Å)
Cite:The Sulfur Atoms of the Substrate Coa and the Catalytic Cysteine are Required for a Productive Mode of Substrate Binding in Bacterial Biosynthetic Thiolase, a Thioester-Dependent Enzyme.
FEBS J., 275, 2008
2VEK
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BU of 2vek by Molmil
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
2V0T
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BU of 2v0t by Molmil
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
2VEI
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BU of 2vei by Molmil
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
2V2D
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BU of 2v2d by Molmil
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
2VEL
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BU of 2vel by Molmil
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
2VTZ
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BU of 2vtz by Molmil
Biosynthetic thiolase from Z. ramigera. Complex of the C89A mutant with coenzyme A.
Descriptor: ACETYL-COA ACETYLTRANSFERASE, COENZYME A, SULFATE ION
Authors:Kursula, P, Merilainen, G, Wierenga, R.K.
Deposit date:2008-05-19
Release date:2008-10-28
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:The Sulfur Atoms of the Substrate Coa and the Catalytic Cysteine are Required for a Productive Mode of Substrate Binding in Bacterial Biosynthetic Thiolase, a Thioester-Dependent Enzyme.
FEBS J., 275, 2008
2X58
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BU of 2x58 by Molmil
The crystal structure of MFE1 liganded with CoA
Descriptor: ADENOSINE-5'-DIPHOSPHATE, COENZYME A, GLYCEROL, ...
Authors:Kasaragod, P, Venkatesan, R, Kiema, T.R, Hiltunen, J.K, Wierenga, R.K.
Deposit date:2010-02-05
Release date:2010-05-12
Last modified:2023-12-20
Method:X-RAY DIFFRACTION (2.8 Å)
Cite:The Crystal Structure of Liganded Rat Peroxisomal Multifunctional Enzyme Type 1: A Flexible Molecule with Two Interconnected Active Sites
J.Biol.Chem., 285, 2010
1SSG
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BU of 1ssg by Molmil
Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase
Descriptor: 2-PHOSPHOGLYCOLIC ACID, GLYCEROL, SULFATE ION, ...
Authors:Kursula, I, Salin, M, Sun, J, Norledge, B.V, Haapalainen, A.M, Sampson, N.S, Wierenga, R.K.
Deposit date:2004-03-24
Release date:2004-08-24
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2.9 Å)
Cite:Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase
Protein Eng.Des.Sel., 17, 2004
1TRD
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BU of 1trd by Molmil
THE INFLUENCE OF CRYSTAL PACKING ON CRYSTALLOGRAPHIC BINDING STUDIES: A NEW CRYSTAL FORM OF TRYPANOSOMAL TIM
Descriptor: PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Noble, M.E.M, Wierenga, R.K.
Deposit date:1992-10-06
Release date:1993-10-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:Structures of the "open" and "closed" state of trypanosomal triosephosphate isomerase, as observed in a new crystal form: implications for the reaction mechanism.
Proteins, 16, 1993
1TPE
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BU of 1tpe by Molmil
COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS
Descriptor: TRIOSEPHOSPHATE ISOMERASE
Authors:Noble, M.E.M, Radha Kishan, K.V, Zeelen, J.Ph, Wierenga, R.K.
Deposit date:1994-02-28
Release date:1994-05-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
Protein Sci., 3, 1994
1TPF
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BU of 1tpf by Molmil
COMPARISON OF THE STRUCTURES AND THE CRYSTAL CONTACTS OF TRYPANOSOMAL TRIOSEPHOSPHATE ISOMERASE IN FOUR DIFFERENT CRYSTAL FORMS
Descriptor: DIMETHYL SULFOXIDE, TRIOSEPHOSPHATE ISOMERASE
Authors:Radha Kishan, K.V, Zeelen, J.Ph, Wierenga, R.K.
Deposit date:1994-02-28
Release date:1994-05-31
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Comparison of the structures and the crystal contacts of trypanosomal triosephosphate isomerase in four different crystal forms.
Protein Sci., 3, 1994
1TTI
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BU of 1tti by Molmil
THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8
Descriptor: 2-PHOSPHOGLYCOLIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Radha Kishan, K.V, Wierenga, R.K.
Deposit date:1995-04-19
Release date:1995-10-15
Last modified:2024-02-14
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:Three new crystal structures of point mutation variants of monoTIM: conformational flexibility of loop-1, loop-4 and loop-8.
Structure, 3, 1995
1SQ7
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BU of 1sq7 by Molmil
Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase
Descriptor: Triosephosphate isomerase
Authors:Kursula, I, Salin, M, Sun, J, Norledge, B.V, Haapalainen, A.M, Sampson, N.S, Wierenga, R.K.
Deposit date:2004-03-18
Release date:2004-08-24
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2.85 Å)
Cite:Understanding protein lids: structural analysis of active hinge mutants in triosephosphate isomerase
Protein Eng.Des.Sel., 17, 2004

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