1CSK
 
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1DCI
 | | DIENOYL-COA ISOMERASE | | Descriptor: | 1,2-ETHANEDIOL, DIENOYL-COA ISOMERASE, MAGNESIUM ION, ... | | Authors: | Modis, Y, Filppula, S.A, Novikov, D, Norledge, B, Hiltunen, J.K, Wierenga, R.K. | | Deposit date: | 1998-02-13 | | Release date: | 1999-03-30 | | Last modified: | 2024-02-07 | | Method: | X-RAY DIFFRACTION (1.5 Å) | | Cite: | The crystal structure of dienoyl-CoA isomerase at 1.5 A resolution reveals the importance of aspartate and glutamate sidechains for catalysis.
Structure, 6, 1998
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2GD0
 | | 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
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2GD6
 | | 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
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4B3J
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2GCE
 | | 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
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4B3I
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2GCI
 | | 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
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2GD2
 | | 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
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1E15
 | | Chitinase B from Serratia Marcescens | | Descriptor: | CHITINASE B | | Authors: | Van Aalten, D.M.F, Synstad, B, Brurberg, M.B, Hough, E, Riise, B.W, Eijsink, V.G.H, Wierenga, R.K. | | Deposit date: | 2000-04-18 | | Release date: | 2000-08-18 | | Last modified: | 2019-07-24 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | Structure of a Two-Domain Chitotriosidase from Serratia Marcescens at 1.9 Angstrom Resoltuion
Proc.Natl.Acad.Sci.USA, 97, 2000
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4BTB
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4BT9
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4BT8
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4BTA
 | | CRYSTAL STRUCTURE OF THE PEPTIDE(PRO-PRO-GLY)3 BOUND COMPLEX OF N- TERMINAL DOMAIN AND PEPTIDE SUBSTRATE BINDING DOMAIN OF PROLYL-4 HYDROXYLASE (RESIDUES 1-244) TYPE I FROM HUMAN | | Descriptor: | PROLINE RICH PEPTIDE, PROLYL 4-HYDROXYLASE SUBUNIT ALPHA-1 | | Authors: | Anantharajan, J, Koski, M.K, Pekkala, M, Wierenga, R.K. | | Deposit date: | 2013-06-14 | | Release date: | 2013-10-09 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (2.95 Å) | | Cite: | The Structural Motifs for Substrate Binding and Dimerization of the Alpha Subunit of Collagen Prolyl 4-Hydroxylase
Structure, 21, 2013
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4CQM
 | | Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD and NADP | | Descriptor: | 1,2-ETHANEDIOL, ACETATE ION, CARBONYL REDUCTASE FAMILY MEMBER 4, ... | | Authors: | Venkatesan, R, SahTeli, S.K, Awoniyi, L.O, Jiang, G, Prus, P, Kastoniotis, A.J, Hiltunen, J.K, Wierenga, R.K, Chen, Z. | | Deposit date: | 2014-02-19 | | Release date: | 2014-09-10 | | Last modified: | 2014-09-17 | | Method: | X-RAY DIFFRACTION (2.339 Å) | | Cite: | Insights Into Mitochondrial Fatty Acid Synthesis from the Structure of Heterotetrameric 3-Ketoacyl-Acp Reductase/3R-Hydroxyacyl-Coa Dehydrogenase.
Nat.Commun., 5, 2014
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2IB9
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2IBY
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2IB7
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2IBU
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2IBW
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2IB8
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4CQL
 | | Crystal structure of heterotetrameric human ketoacyl reductase complexed with NAD | | Descriptor: | CARBONYL REDUCTASE FAMILY MEMBER 4, ESTRADIOL 17-BETA-DEHYDROGENASE 8, NICOTINAMIDE-ADENINE-DINUCLEOTIDE | | Authors: | Venkatesan, R, Sah-Teli, S.K, Awoniyi, L.O, Jiang, G, Prus, P, Kastaniotis, A.J, Hiltunen, J.K, Wierenga, R.K, Chen, Z. | | Deposit date: | 2014-02-19 | | Release date: | 2014-09-10 | | Last modified: | 2023-12-20 | | Method: | X-RAY DIFFRACTION (2.85 Å) | | Cite: | Insights Into Mitochondrial Fatty Acid Synthesis from the Structure of Heterotetrameric 3-Ketoacyl-Acp Reductase/3R-Hydroxyacyl-Coa Dehydrogenase.
Nat.Commun., 5, 2014
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2J24
 | | 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
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2J27
 | | 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: | 2023-12-13 | | Method: | X-RAY DIFFRACTION (1.15 Å) | | Cite: | Functional Role of the Conserved Active Site Proline of Triosephosphate Isomerase.
Biochemistry, 45, 2006
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1GU7
 | | Enoyl thioester reductase from Candida tropicalis | | Descriptor: | ENOYL-[ACYL-CARRIER-PROTEIN] REDUCTASE [NADPH, B-SPECIFIC] 1,MITOCHONDRIAL, GLYCEROL, ... | | Authors: | Airenne, T.T, Torkko, J.M, Wierenga, R.K, Hiltunen, J.K. | | Deposit date: | 2002-01-24 | | Release date: | 2003-03-13 | | Last modified: | 2019-07-24 | | Method: | X-RAY DIFFRACTION (1.7 Å) | | Cite: | Structure-Function Analysis of Enoyl Thioester Reductase Involved in Mitochondrial Maintenance
J.Mol.Biol., 327, 2003
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