Copper in PDB 1rk5: The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2

All present enzymatic activity of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2:
3.5.1.81;

The structure of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2, PDB code: 1rk5 was solved by W.L.Lai, L.Y.Chou, C.Y.Ting, Y.C.Tsai, S.H.Liaw, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.40 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.016, 77.266, 135.982, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 20.4

The binding sites of Copper atom in the The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2 (pdb code 1rk5). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2, PDB code: 1rk5:

Copper binding site 1 out of 1 in the The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The D-Aminoacylase Mutant D366A in Complex with 100MM CUCL2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu602 b:10.2 occ:1.00 NE2 A:HIS69 2.0 14.4 1.0 NE2 A:HIS67 2.1 7.3 1.0 SG A:CYS96 2.3 8.0 1.0 CE1 A:HIS69 2.4 16.5 1.0 OXT A:ACT901 2.5 15.0 1.0 CE1 A:HIS67 2.9 7.7 1.0 C A:ACT901 3.1 17.7 1.0 CD2 A:HIS67 3.2 7.3 1.0 ZN A:ZN601 3.2 10.5 1.0 CD2 A:HIS69 3.3 13.7 1.0 CB A:CYS96 3.5 9.0 1.0 O A:ACT901 3.5 16.5 1.0 ND1 A:HIS69 3.7 14.8 1.0 CB A:ASN95 3.8 8.9 1.0 CH3 A:ACT901 3.9 17.3 1.0 ND1 A:HIS67 4.1 6.7 1.0 CG A:HIS69 4.1 12.2 1.0 CD2 A:HIS250 4.2 10.3 1.0 CG A:HIS67 4.2 6.8 1.0 NE2 A:HIS250 4.3 10.8 1.0 C A:ASN95 4.3 7.9 1.0 N A:CYS96 4.3 7.8 1.0 O A:ASN95 4.5 7.2 1.0 CA A:CYS96 4.6 8.6 1.0 CA A:ASN95 4.7 7.9 1.0 CG A:ASN95 5.0 9.4 1.0

W.L.Lai, L.Y.Chou, C.Y.Ting, R.Kirby, Y.C.Tsai, A.H.Wang, S.H.Liaw. The Functional Role of the Binuclear Metal Center in D-Aminoacylase: One-Metal Activation and Second-Metal Attenuation. J.Biol.Chem. V. 279 13962 2004.
ISSN: ISSN 0021-9258
PubMed: 14736882
DOI: 10.1074/JBC.M308849200