2apr

STRUCTURE AND REFINEMENT AT 1.8 ANGSTROMS RESOLUTION OF THE ASPARTIC PROTEINASE FROM RHIZOPUS CHINENSIS

spinqualitylabelsall models 2apr, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2apr is a 1 chain structure with sequence from Atcc 52807. This structure supersedes the now removed PDB entry 1apr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Activity: Hydrolase, with EC number 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure of rhizopuspepsin (EC 3.4.23.6), the aspartic proteinase from Rhizopus chinensis, has been refined to a crystallographic R-factor of 0.143 at 1.8 A resolution. The positions of 2417 protein atoms have been determined with a root-mean-square (r.m.s.) error of 0.12 A. In the final model, the r.m.s. deviation from ideality for bond distances is 0.010 A, and for angle distances it is 0.034 A. During the course of the refinement, a calcium ion and 373 water molecules, of which 17 are internal, have been located. The active aspartate residues, Asp35 and Asp218, are involved in similar hydrogen-bonding interactions with neighboring residues and with several water molecules. One water molecule is located between the two carboxyl groups of the catalytic aspartate residues in a tightly hydrogen-bonded position. The refinement resulted in an unambiguous interpretation of the highly mobile "flap", a beta-hairpin loop region that projects over the binding pocket. Large solvent channels are formed when the molecules pack in the crystal, exposing the binding pocket and making it easily accessible. Intermolecular contacts involve mainly solvent molecules and a few protein atoms. The three-dimensional structure of rhizopuspepsin closely resembles other aspartic proteinase structures. A detailed comparison with the structure of penicillopepsin showed striking similarities as well as subtle differences in the active site geometry and molecular packing. Structure and refinement at 1.8 A resolution of the aspartic proteinase from Rhizopus chinensis.,Suguna K, Bott RR, Padlan EA, Subramanian E, Sheriff S, Cohen GH, Davies DR J Mol Biol. 1987 Aug 20;196(4):877-900. PMID:3316666 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pepsin Proteinase

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