1H1N
Atomic resolution structure of the major endoglucanase from Thermoascus aurantiacus
Summary for 1H1N
| Entry DOI | 10.2210/pdb1h1n/pdb |
| Descriptor | ENDO TYPE CELLULASE ENGI (2 entities in total) |
| Functional Keywords | hydrolase, glycosyl hydrolase, family 5, subtype, thermophilic, thermophile, endoglucanase |
| Biological source | THERMOASCUS AURANTIACUS |
| Total number of polymer chains | 2 |
| Total formula weight | 67462.60 |
| Authors | Van Petegem, F.,Vandenberghe, I.,Bhat, M.K.,Van Beeumen, J. (deposition date: 2002-07-19, release date: 2002-08-12, Last modification date: 2024-11-06) |
| Primary citation | Van Petegem, F.,Vandenberghe, I.,Bhat, M.K.,Van Beeumen, J. Atomic Resolution Structure of the Major Endoglucanase from Thermoascus Aurantiacus Biochem.Biophys.Res.Commun., 296:161-, 2002 Cited by PubMed Abstract: The crystal structure of the major endoglucanase from the thermophilic fungus Thermoascus aurantiacus was determined by single isomorphous replacement at 1.12A resolution. The full sequence supports the classification of the protein in a subgroup of glycoside hydrolase family 5 for which no structural data are available yet. The active site shows eight critical residues, strictly conserved within family 5. In addition, aromatic residues that line the substrate-binding cleft and that are possibly involved in substrate-binding are identified. A number of residues seem to be conserved among members of the subtype, including a disulphide bridge between Cys212 and Cys249. PubMed: 12147244DOI: 10.1016/S0006-291X(02)00775-1 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.12 Å) |
Structure validation
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