1aac | pdb_00001aac

AMICYANIN OXIDIZED, 1.31 ANGSTROMS

spinqualitylabelsall models 1aac, resolution 1.31Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1aac is a 1 chain structure with sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU Resources: FirstGlance, OCA, RCSB, PDBsum 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 High-resolution X-ray diffraction data to d(min) = 1.31 A were collected on a Xuong-Hamlin area detector from crystals of the blue-copper protein amicyanin, isolated from P. denitrificans. With coordinates from the earlier 2.0 A structure determination as a starting point, simulated annealing and restrained positional and temperature factor refinements using the program X-PLOR resulted in a final R factor of 15.5%, based on 21 131 unique reflections in the range 8.0-1.3 A. Comparison of the 1.31 A structure with that at 2.0 A shows the same basic features. However, the high-resolution electron-density maps clearly reveal additional solvent molecules and significant discrete disorder in protein side chains and within the solvent structure. As a consequence of modelling side-chain disorder, several new hydrogen-bonding interactions were identified. X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 A resolution.,Cunane LM, Chen ZW, Durley RC, Mathews FS Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):676-86. PMID:15299631 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA