2asi
From Proteopedia
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ASPARTIC PROTEINASE
Overview
The crystal structure of the aspartic proteinase from Rhizomucor miehei, (RMP, EC 3. 4. 23. 23) has been refined to 2.15 A resolution to a, crystallographic R-value of 0.215 and an Rfree of 0.281. The, root-mean-square (r.m.s.) error for the atomic coordinates estimated from, a Luzzati plot is 0.2 A. The r.m.s. deviations for the bond distances and, bond angles from ideality are 0.01 A and 1.7 degrees, respectively. RMP, contains two domains that consist predominantly of beta-sheets. A large, substrate-binding cleft is clearly visible between the two domains, and, the two catalytic residues Asp38 and Asp237 are located in the middle of, the cleft with a water molecule bridging the carboxyl groups of Asp38 and, Asp237. Due to crystal packing, the C-terminal domain is more mobile than, the ... [(full description)]
About this Structure
2ASI is a [Single protein] structure of sequence from [Rhizomucor miehei] with NAG as [ligand]. This structure superseeds the now removed PDB entry 1ASI. Active as [Hydrolase], with EC number [3.4.23.23]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the aspartic proteinase from Rhizomucor miehei at 2.15 A resolution., Yang J, Teplyakov A, Quail JW, J Mol Biol. 1997 May 2;268(2):449-59. PMID:9159482
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