Copper in PDB 2gb2: The P52G Mutant of Amicyanin in the Cu(II) State.

The structure of The P52G Mutant of Amicyanin in the Cu(II) State., PDB code: 2gb2 was solved by J.K.Ma, C.J.Carrell, F.S.Mathews, V.L.Davidson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	28.470, 55.650, 27.090, 90.00, 95.08, 90.00
R / Rfree (%)	13 / 18.4

The binding sites of Copper atom in the The P52G Mutant of Amicyanin in the Cu(II) State. (pdb code 2gb2). 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 P52G Mutant of Amicyanin in the Cu(II) State., PDB code: 2gb2:

Copper binding site 1 out of 1 in the The P52G Mutant of Amicyanin in the Cu(II) State.


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of The P52G Mutant of Amicyanin in the Cu(II) State. within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu107 b:20.7 occ:1.00 ND1 A:HIS53 2.0 18.5 1.0 ND1 A:HIS95 2.1 17.6 1.0 SG A:CYS92 2.2 16.9 1.0 CE1 A:HIS53 2.9 19.8 1.0 SD A:MET98 2.9 17.9 1.0 CG A:HIS53 3.0 18.4 1.0 CE1 A:HIS95 3.1 18.4 1.0 CG A:HIS95 3.1 17.2 1.0 CB A:CYS92 3.2 14.5 1.0 CB A:HIS95 3.4 19.3 1.0 CB A:HIS53 3.4 17.7 1.0 CA A:HIS53 3.6 16.5 1.0 CE A:MET98 3.7 28.2 1.0 O A:GLY52 3.8 20.9 1.0 NE2 A:HIS53 4.0 22.6 1.0 CD2 A:HIS53 4.1 21.8 1.0 NE2 A:HIS95 4.2 18.7 1.0 CD2 A:HIS95 4.3 19.5 1.0 CG A:PRO94 4.3 21.2 1.0 N A:HIS95 4.4 17.0 1.0 CG A:MET98 4.4 17.5 1.0 CA A:HIS95 4.5 16.1 1.0 N A:HIS53 4.5 19.8 1.0 C A:GLY52 4.6 22.2 1.0 CA A:CYS92 4.6 13.3 1.0 N A:ASN54 4.6 14.3 1.0 C A:HIS53 4.7 16.8 1.0 CE A:MET28 4.8 30.3 1.0 O A:HIS95 4.9 17.8 1.0 CB A:MET98 4.9 17.2 1.0 CD A:PRO94 4.9 16.5 1.0

J.K.Ma, C.J.Carrell, F.S.Mathews, V.L.Davidson. Site-Directed Mutagenesis of Proline 52 to Glycine in Amicyanin Converts A True Electron Transfer Reaction Into One That Is Conformationally Gated. Biochemistry V. 45 8284 2006.
ISSN: ISSN 0006-2960
PubMed: 16819827
DOI: 10.1021/BI0605134