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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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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1AW2
| 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
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1AW1
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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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1TTJ
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2X1R
| Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase | Descriptor: | 3-(PROPYLSULFONYL)PROPANOIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE, ... | Authors: | Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R. | Deposit date: | 2010-01-04 | Release date: | 2010-01-26 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (1.98 Å) | Cite: | Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase Acta Crystallogr.,Sect.D, 66, 2010
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2X1S
| Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase | Descriptor: | 3-SULFOPROPANOIC ACID, SULFATE ION, TRIOSEPHOSPHATE ISOMERASE, ... | Authors: | Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Castejeijn, M.G, Neubauer, P, Salmon, L, Wierenga, R. | Deposit date: | 2010-01-04 | Release date: | 2010-01-26 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (1.93 Å) | Cite: | Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase Acta Crystallogr.,Sect.D, 66, 2010
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2X2G
| CRYSTALLOGRAPHIC BINDING STUDIES WITH AN ENGINEERED MONOMERIC VARIANT OF TRIOSEPHOSPHATE ISOMERASE | Descriptor: | 3-PHOSPHOGLYCERIC ACID, TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL | Authors: | Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R. | Deposit date: | 2010-01-13 | Release date: | 2010-01-26 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (1.9 Å) | Cite: | Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase Acta Crystallogr.,Sect.D, 66, 2010
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2X1U
| Crystallographic binding studies with an engineered monomeric variant of triosephosphate isomerase | Descriptor: | SULFATE ION, TRIOSEPHOSPHATE ISOMERASE, GLYCOSOMAL | Authors: | Salin, M, Kapetaniou, E.G, Vaismaa, M, Lajunen, M, Casteleijn, M.G, Neubauer, P, Salmon, L, Wierenga, R. | Deposit date: | 2010-01-04 | Release date: | 2010-01-26 | Last modified: | 2023-12-20 | Method: | X-RAY DIFFRACTION (1.84 Å) | Cite: | Crystallographic Binding Studies with an Engineered Monomeric Variant of Triosephosphate Isomerase Acta Crystallogr.,Sect.D, 66, 2010
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4BTB
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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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1CSK
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1OU6
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2IB9
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2IBY
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2IB8
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2IB7
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2IBU
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2IBW
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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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1M4S
| Biosynthetic thiolase, Cys89 acetylated, unliganded form | Descriptor: | Acetyl-CoA acetyltransferase, GLYCEROL, SULFATE ION | Authors: | Kursula, P, Ojala, J, Lambeir, A.-M, Wierenga, R.K. | Deposit date: | 2002-07-03 | Release date: | 2002-11-29 | Last modified: | 2024-10-30 | Method: | X-RAY DIFFRACTION (1.87 Å) | Cite: | The catalytic cycle of biosynthetic thiolase: A conformational
journey of an acetyl group through four binding modes and two oxyanion holes Biochemistry, 41, 2002
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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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