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PDB: 220 results

2WL5
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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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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
2WKU
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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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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
6TP5
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Crystal structure of human Transmembrane prolyl 4-hydroxylase
Descriptor: 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, CHLORIDE ION, ...
Authors:Myllykoski, M, Sutinen, A, Koski, M.K, Kallio, J.P, Raasakka, A, Myllyharju, J, Wierenga, R.K, Koivunen, P.
Deposit date:2019-12-12
Release date:2020-12-23
Last modified:2024-10-23
Method:X-RAY DIFFRACTION (2.25 Å)
Cite:Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains.
J.Biol.Chem., 296, 2020
1TTJ
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THREE NEW CRYSTAL STRUCTURES OF POINT MUTATION VARIANTS OF MONOTIM: CONFORMATIONAL FLEXIBILITY OF LOOP-1,LOOP-4 AND LOOP-8
Descriptor: PHOSPHOGLYCOLOHYDROXAMIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Radha Kishan, K.V, Wierenga, R.K.
Deposit date:1995-04-20
Release date:1995-09-15
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
1AFW
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THE 1.8 ANGSTROM CRYSTAL STRUCTURE OF THE DIMERIC PEROXISOMAL THIOLASE OF SACCHAROMYCES CEREVISIAE
Descriptor: (4R)-2-METHYLPENTANE-2,4-DIOL, 3-KETOACETYL-COA THIOLASE
Authors:Mathieu, M, Wierenga, R.K.
Deposit date:1997-03-15
Release date:1997-06-16
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:The 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism.
J.Mol.Biol., 273, 1997
1AW2
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TRIOSEPHOSPHATE ISOMERASE OF VIBRIO MARINUS
Descriptor: SULFATE ION, TRIOSEPHOSPHATE ISOMERASE
Authors:Maes, D, Zeelen, J.P, Wierenga, R.K.
Deposit date:1997-10-09
Release date:1998-01-28
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (2.65 Å)
Cite:Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
J.Biol.Chem., 273, 1998
1B9B
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TRIOSEPHOSPHATE ISOMERASE OF THERMOTOGA MARITIMA
Descriptor: PROTEIN (TRIOSEPHOSPHATE ISOMERASE), SULFATE ION
Authors:Maes, D, Wierenga, R.K.
Deposit date:1999-02-09
Release date:2000-01-01
Last modified:2024-10-16
Method:X-RAY DIFFRACTION (2.85 Å)
Cite:The crystal structure of triosephosphate isomerase (TIM) from Thermotoga maritima: a comparative thermostability structural analysis of ten different TIM structures.
Proteins, 37, 1999
1AW1
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TRIOSEPHOSPHATE ISOMERASE OF VIBRIO MARINUS COMPLEXED WITH 2-PHOSPHOGLYCOLATE
Descriptor: 2-PHOSPHOGLYCOLIC ACID, TRIOSEPHOSPHATE ISOMERASE
Authors:Maes, D, Zeelen, J.P, Wierenga, R.K.
Deposit date:1997-10-09
Release date:1998-01-28
Last modified:2024-05-22
Method:X-RAY DIFFRACTION (2.7 Å)
Cite:Triose-phosphate isomerase (TIM) of the psychrophilic bacterium Vibrio marinus. Kinetic and structural properties.
J.Biol.Chem., 273, 1998
1CSK
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THE CRYSTAL STRUCTURE OF HUMAN CSKSH3: STRUCTURAL DIVERSITY NEAR THE RT-SRC AND N-SRC LOOP
Descriptor: C-SRC SH3 DOMAIN
Authors:Mathieu, M, Wierenga, R.K.
Deposit date:1994-03-22
Release date:1994-07-31
Last modified:2024-02-07
Method:X-RAY DIFFRACTION (2.5 Å)
Cite:The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop.
FEBS Lett., 341, 1994
2IB9
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Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase (T2): the importance of potassium and chloride for its structure and function
Descriptor: 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, Acetyl-CoA acetyltransferase, CHLORIDE ION, ...
Authors:Haapalainen, A.M, Wierenga, R.K.
Deposit date:2006-09-11
Release date:2007-04-03
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2.05 Å)
Cite:Crystallographic and Kinetic Studies of Human Mitochondrial Acetoacetyl-CoA Thiolase: The Importance of Potassium and Chloride Ions for Its Structure and Function
Biochemistry, 46, 2007
2IBY
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Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase (T2): the importance of potassium and chloride for its structure and function
Descriptor: 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, Acetyl-CoA acetyltransferase, CHLORIDE ION, ...
Authors:Haapalainen, A.M, Wierenga, R.K.
Deposit date:2006-09-12
Release date:2007-04-03
Last modified:2023-11-15
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Crystallographic and Kinetic Studies of Human Mitochondrial Acetoacetyl-CoA Thiolase: The Importance of Potassium and Chloride Ions for Its Structure and Function
Biochemistry, 46, 2007
2IB8
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BU of 2ib8 by Molmil
Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase (T2): the importance of potassium and chloride for its structure and function
Descriptor: 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, Acetyl-CoA acetyltransferase, CHLORIDE ION, ...
Authors:Haapalainen, A.M, Wierenga, R.K.
Deposit date:2006-09-11
Release date:2007-04-03
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:Crystallographic and Kinetic Studies of Human Mitochondrial Acetoacetyl-CoA Thiolase: The Importance of Potassium and Chloride Ions for Its Structure and Function
Biochemistry, 46, 2007
2IB7
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BU of 2ib7 by Molmil
Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase (T2): the importance of potassium and chloride for its structure and function
Descriptor: 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, Acetyl-CoA acetyltransferase, CHLORIDE ION, ...
Authors:Haapalainen, A.M, Wierenga, R.K.
Deposit date:2006-09-11
Release date:2007-04-03
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2.05 Å)
Cite:Crystallographic and Kinetic Studies of Human Mitochondrial Acetoacetyl-CoA Thiolase: The Importance of Potassium and Chloride Ions for Its Structure and Function
Biochemistry, 46, 2007
2IBU
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Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase (T2): the importance of potassium and chloride for its structure and function
Descriptor: Acetyl-CoA acetyltransferase, CHLORIDE ION, COENZYME A, ...
Authors:Haapalainen, A.M, Wierenga, R.K.
Deposit date:2006-09-12
Release date:2007-04-03
Last modified:2024-10-30
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Crystallographic and Kinetic Studies of Human Mitochondrial Acetoacetyl-CoA Thiolase: The Importance of Potassium and Chloride Ions for Its Structure and Function
Biochemistry, 46, 2007
2IBW
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BU of 2ibw by Molmil
Crystallographic and kinetic studies of human mitochondrial acetoacetyl-CoA thiolase (T2): the importance of potassium and chloride for its structure and function
Descriptor: 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, Acetyl-CoA acetyltransferase, CHLORIDE ION, ...
Authors:Haapalainen, A.M, Wierenga, R.K.
Deposit date:2006-09-12
Release date:2007-04-03
Last modified:2024-10-30
Method:X-RAY DIFFRACTION (1.9 Å)
Cite:Crystallographic and Kinetic Studies of Human Mitochondrial Acetoacetyl-CoA Thiolase: The Importance of Potassium and Chloride Ions for Its Structure and Function
Biochemistry, 46, 2007
2GD0
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The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
Descriptor: (S)-2-METHYLMYRISTOYL-COENZYME A, GLYCEROL, probable alpha-methylacyl-CoA racemase MCR
Authors:Bhaumik, P, Wierenga, R.K.
Deposit date:2006-03-15
Release date:2007-02-20
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface
J.Mol.Biol., 367, 2007
2GD6
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The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
Descriptor: ACETYL COENZYME *A, GLYCEROL, probable alpha-methylacyl-CoA racemase MCR
Authors:Bhaumik, P, Wierenga, R.K.
Deposit date:2006-03-15
Release date:2007-02-20
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (2.3 Å)
Cite:The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface
J.Mol.Biol., 367, 2007
2GCE
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The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
Descriptor: (R)-IBUPROFENOYL-COENZYME A, (S)-IBUPROFENOYL-COENZYME A, probable alpha-methylacyl-CoA racemase MCR
Authors:Bhaumik, P, Wierenga, R.K.
Deposit date:2006-03-14
Release date:2007-02-20
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface
J.Mol.Biol., 367, 2007
2J24
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The functional role of the conserved active site proline of triosephosphate isomerase
Descriptor: TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL
Authors:Casteleijn, M.G, Alahuhta, M, Groebel, K, El-Sayed, I, Augustyns, K, Lambeir, A.M, Neubauer, P, Wierenga, R.K.
Deposit date:2006-08-16
Release date:2007-01-02
Last modified:2023-12-13
Method:X-RAY DIFFRACTION (2.1 Å)
Cite:Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase.
Biochemistry, 45, 2006
2J27
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The functional role of the conserved active site proline of triosephosphate isomerase.
Descriptor: 2-PHOSPHOGLYCOLIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE GLYCOSOMAL
Authors:Casteleijn, M.G, Alahuhta, M, Groebel, K, El-Sayed, I, Augustyns, K, Lambeir, A.M, Neubauer, P, Wierenga, R.K.
Deposit date:2006-08-16
Release date:2007-01-02
Last modified:2024-05-01
Method:X-RAY DIFFRACTION (1.15 Å)
Cite:Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase.
Biochemistry, 45, 2006
2GCI
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The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an asparte/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
Descriptor: (R)-2-METHYLMYRISTOYL-COENZYME A, GLYCEROL, probable alpha-methylacyl-CoA racemase MCR
Authors:Bhaumik, P, Wierenga, R.K.
Deposit date:2006-03-14
Release date:2007-02-20
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (1.6 Å)
Cite:The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface
J.Mol.Biol., 367, 2007
2GD2
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The 1,1-proton transfer reaction mechanism by alpha-methylacyl-CoA racemase is catalyzed by an aspartate/histidine pair and involves a smooth, methionine-rich surface for binding the fatty acyl moiety
Descriptor: ACETOACETYL-COENZYME A, GLYCEROL, probable alpha-methylacyl-CoA racemase MCR
Authors:Bhaumik, P, Wierenga, R.K.
Deposit date:2006-03-15
Release date:2007-02-20
Last modified:2023-10-25
Method:X-RAY DIFFRACTION (1.7 Å)
Cite:The Catalysis of the 1,1-Proton Transfer by alpha-Methyl-acyl-CoA Racemase Is Coupled to a Movement of the Fatty Acyl Moiety Over a Hydrophobic, Methionine-rich Surface
J.Mol.Biol., 367, 2007
2JIG
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Crystal structure of Chlamydomonas reinhardtii prolyl-4 hydroxylase type I complexed with zinc and pyridine-2,4-dicarboxylate
Descriptor: GLYCEROL, PROLYL-4 HYDROXYLASE, PYRIDINE-2,4-DICARBOXYLIC ACID, ...
Authors:Koski, M.K, Hieta, R, Bollner, C, Kivirikko, K.I, Myllyharju, J, Wierenga, R.K.
Deposit date:2007-06-28
Release date:2007-10-30
Last modified:2024-10-23
Method:X-RAY DIFFRACTION (1.85 Å)
Cite:The Active Site of an Algal Prolyl 4-Hydroxylase Has a Large Structural Plasticity.
J.Biol.Chem., 282, 2007

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