1AAC

AMICYANIN OXIDIZED, 1.31 ANGSTROMS

Summary for 1AAC

• Entry DOI: 10.2210/pdb1aac/pdb
• Descriptor: AMICYANIN, COPPER (II) ION (3 entities in total)
• Functional Keywords: electron transport
• Biological source: Paracoccus denitrificans
• Cellular location: Periplasm: P22364
• Total number of polymer chains: 1
• Total formula weight: 11568.72

Authors

Cunane, L.M.,Chen, Z.-W.,Durley, R.C.E.,Mathews, F.S. (deposition date: 1995-09-07, release date: 1996-03-08, Last modification date: 2024-02-07)

Primary citation

Cunane, L.M.,Chen, Z.W.,Durley, R.C.,Mathews, F.S.
X-ray structure of the cupredoxin amicyanin, from Paracoccus denitrificans, refined at 1.31 A resolution.
Acta Crystallogr.,Sect.D, 52:676-686, 1996

PubMed Abstract: 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.

PubMed: 15299631
DOI: 10.1107/S0907444996001072

Experimental method

X-RAY DIFFRACTION (1.31 Å)