1ZJK
| Crystal structure of the zymogen catalytic region of human MASP-2 | Descriptor: | Mannan-binding lectin serine protease 2 | Authors: | Gal, P, Harmat, V, Kocsis, A, Bian, T, Barna, L, Ambrus, G, Vegh, B, Balczer, J, Sim, R.B, Naray-Szabo, G, Zavodszky, P. | Deposit date: | 2005-04-29 | Release date: | 2005-07-26 | Last modified: | 2024-10-30 | Method: | X-RAY DIFFRACTION (2.18 Å) | Cite: | A True Autoactivating Enzyme: Structural insight into mannose-binding lectin-associated serine protease-2 activations J.Biol.Chem., 280, 2005
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1Q3X
| Crystal structure of the catalytic region of human MASP-2 | Descriptor: | GLYCEROL, Mannan-binding lectin serine protease 2, SODIUM ION | Authors: | Harmat, V, Gal, P, Kardos, J, Szilagyi, K, Ambrus, G, Naray-Szabo, G, Zavodszky, P. | Deposit date: | 2003-08-01 | Release date: | 2004-08-03 | Last modified: | 2023-08-16 | Method: | X-RAY DIFFRACTION (2.23 Å) | Cite: | The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions J.Mol.Biol., 342, 2004
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4P58
| Crystal structure of mouse comt bound to an inhibitor | Descriptor: | 1',3'-dimethyl-1H,1'H-3,4'-bipyrazole, Catechol O-methyltransferase | Authors: | Lanier, M. | Deposit date: | 2014-03-15 | Release date: | 2014-06-25 | Last modified: | 2023-09-27 | Method: | X-RAY DIFFRACTION (2.06 Å) | Cite: | A fragment-based approach to identifying S-adenosyl-l-methionine -competitive inhibitors of catechol O-methyl transferase (COMT). J.Med.Chem., 57, 2014
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3NV0
| Crystal structure and mutational analysis of the NXF2/NXT1 heterodimeric complex from caenorhabditis elegans at 1.84 A resolution | Descriptor: | 1,2-ETHANEDIOL, BETA-MERCAPTOETHANOL, DI(HYDROXYETHYL)ETHER, ... | Authors: | Kerkow, D.E, Carmel, A.B, Williamson, J.R. | Deposit date: | 2010-07-07 | Release date: | 2011-07-20 | Last modified: | 2024-02-21 | Method: | X-RAY DIFFRACTION (1.84 Å) | Cite: | The structure of the NXF2/NXT1 heterodimeric complex reveals the combined specificity and versatility of the NTF2-like fold. J.Mol.Biol., 415, 2012
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