Copper in PDB 2idq: Structure of M98A Mutant of Amicyanin, Cu(II)

The structure of Structure of M98A Mutant of Amicyanin, Cu(II), PDB code: 2idq was solved by C.J.Carrell, J.K.Ma, W.Antholine, J.P.Hosler, 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)	30.00 / 0.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	28.570, 56.160, 26.970, 90.00, 96.63, 90.00
R / Rfree (%)	10.8 / 13

The binding sites of Copper atom in the Structure of M98A Mutant of Amicyanin, Cu(II) (pdb code 2idq). 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 M98A Mutant of Amicyanin, Cu(II), PDB code: 2idq:

Copper binding site 1 out of 1 in the Structure of M98A Mutant of Amicyanin, Cu(II)


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of M98A Mutant of Amicyanin, Cu(II) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu107 b:7.5 occ:1.00 ND1 A:HIS53 1.9 7.3 1.0 ND1 A:HIS95 2.0 8.4 1.0 SG A:CYS92 2.1 8.0 1.0 O A:HOH264 2.4 34.3 1.0 CE1 A:HIS53 2.9 8.2 1.0 CE1 A:HIS95 3.0 10.1 1.0 CG A:HIS53 3.0 6.5 1.0 CG A:HIS95 3.1 7.8 1.0 CB A:CYS92 3.3 5.4 1.0 CB A:HIS95 3.4 7.1 1.0 CB A:HIS53 3.4 6.7 1.0 CA A:HIS53 3.6 5.3 1.0 O A:PRO52 3.7 7.8 1.0 NE2 A:HIS53 4.1 8.5 1.0 NE2 A:HIS95 4.1 11.6 1.0 CG A:PRO94 4.1 7.2 1.0 CD2 A:HIS53 4.1 7.2 1.0 CD2 A:HIS95 4.2 11.3 1.0 N A:HIS53 4.4 5.7 1.0 C A:PRO52 4.5 6.4 1.0 N A:HIS95 4.5 6.0 1.0 CA A:HIS95 4.5 6.4 1.0 N A:ASN54 4.5 5.2 1.0 C A:HIS53 4.6 5.4 1.0 CA A:CYS92 4.6 4.7 1.0 CD A:PRO94 4.7 6.3 1.0 C A:CYS92 5.0 5.2 1.0

C.J.Carrell, J.K.Ma, W.E.Antholine, J.P.Hosler, F.S.Mathews, V.L.Davidson. Generation of Novel Copper Sites By Mutation of the Axial Ligand of Amicyanin. Atomic Resolution Structures and Spectroscopic Properties Biochemistry V. 46 1900 2007.
ISSN: ISSN 0006-2960
PubMed: 17295442
DOI: 10.1021/BI0619674