Copper in PDB 3iea: Structure of Reduced M98L Mutant of Amicyanin

The structure of Structure of Reduced M98L Mutant of Amicyanin, PDB code: 3iea was solved by N.Sukumar, V.L.Davidson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.00 / 2.20
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	99.750, 99.750, 70.740, 90.00, 90.00, 120.00
R / Rfree (%)	18.4 / 20

The structure of Structure of Reduced M98L Mutant of Amicyanin also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Zinc	(Zn)	1 atom

The binding sites of Copper atom in the Structure of Reduced M98L Mutant of Amicyanin (pdb code 3iea). 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 Structure of Reduced M98L Mutant of Amicyanin, PDB code: 3iea:

Copper binding site 1 out of 1 in the Structure of Reduced M98L Mutant of Amicyanin


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Reduced M98L Mutant of Amicyanin within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu107 b:46.9 occ:1.00 ND1 A:HIS53 2.2 32.3 1.0 SG A:CYS92 2.2 33.3 1.0 ND1 A:HIS95 2.7 41.8 1.0 CE1 A:HIS53 3.1 30.7 1.0 CB A:CYS92 3.2 29.4 1.0 CG A:HIS53 3.2 32.9 1.0 CD2 A:LEU98 3.5 38.5 1.0 CB A:HIS53 3.6 30.6 1.0 CA A:HIS53 3.6 31.3 1.0 CE1 A:HIS95 3.6 39.8 1.0 O A:PRO52 3.7 30.5 1.0 CG A:HIS95 3.7 36.1 1.0 CB A:HIS95 4.0 32.9 1.0 NE2 A:HIS53 4.2 37.7 1.0 CD2 A:HIS53 4.3 31.7 1.0 N A:HIS53 4.5 28.6 1.0 N A:ASN54 4.5 28.2 1.0 C A:PRO52 4.6 29.0 1.0 CA A:CYS92 4.6 29.5 1.0 CE A:MET28 4.6 46.1 1.0 CD A:PRO94 4.6 34.0 1.0 C A:HIS53 4.6 29.9 1.0 N A:HIS95 4.7 31.1 1.0 CG A:LEU98 4.7 40.5 1.0 NE2 A:HIS95 4.8 40.0 1.0 CG A:PRO94 4.8 39.7 1.0 CD2 A:HIS95 4.9 35.4 1.0 CA A:HIS95 4.9 33.9 1.0 C A:CYS92 4.9 28.4 1.0

M.Choi, N.Sukumar, A.Liu, V.L.Davidson. Defining the Role of the Axial Ligand of the Type 1 Copper Site in Amicyanin By Replacement of Methionine with Leucine. Biochemistry V. 48 9174 2009.
ISSN: ISSN 0006-2960
PubMed: 19715303
DOI: 10.1021/BI900836H