1moo

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spinqualitylabelsall models 1moo, resolution 1.05Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Site Specific Mutant (H64A) of Human Carbonic Anhydrase II at high resolution

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Using synchrotron radiation and a CCD detector, X-ray data have been, collected at 100 K for the His64Ala mutant of human carbonic anhydrase II, complexed with 4-methylimidazole (4-MI) to a maximal 1.05 A resolution, allowing full anisotropic least-squares refinement. The refined model has, a conventional R factor of 15.7% for all reflections. The C(alpha), coordinates of the model presented here have an r.m.s. deviation of 0.10 A, relative to the previously determined structure at 1.6 A resolution., Several amino-acid residues (six of the 255 observed) have been identified, with multiple rotamer side-chain conformations. C, N and O atoms can be, differentiated with selective electron-density map contouring. The, estimated standard deviations for all main-chain non-H atom bond lengths, and angles are 0.013 and 0.030 A, respectively, based on unrestrained, full-matrix least-squares refinement. This structure gives detailed, information about the tetrahedrally arranged zinc ion coordinated by three, histidine N atoms (His94 N(epsilon 2), His96 N(epsilon2) and His119, N(delta1)) and a water/hydroxide, the multiple binding sites of the proton, chemical rescue molecule 4-MI and the solvent networks linking the, zinc-bound water/hydroxide and 4-MI molecules. This structure presents the, highest resolution structure of a carbonic anhydrase isozyme so far, determined and adds to the understanding of proton-transfer processes.

Disease

Known disease associated with this structure: Osteopetrosis, autosomal recessive 3, with renal tubular acidosis OMIM:[611492]

About this Structure

1MOO is a Single protein structure of sequence from Homo sapiens with ZN, HG and 4MZ as ligands. Active as Carbonate dehydratase, with EC number 4.2.1.1 Full crystallographic information is available from OCA.

Reference

The refined atomic structure of carbonic anhydrase II at 1.05 A resolution: implications of chemical rescue of proton transfer., Duda D, Govindasamy L, Agbandje-McKenna M, Tu C, Silverman DN, McKenna R, Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):93-104. Epub 2002, Dec 19. PMID:12499545

Page seeded by OCA on Mon Nov 12 18:13:22 2007