Copper in PDB 2ft7: Structure of Cu(I)Azurin at pH 6, with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Ctphpm"

The structure of Structure of Cu(I)Azurin at pH 6, with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Ctphpm", PDB code: 2ft7 was solved by M.J.Banfield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.80 / 1.40
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	51.957, 51.957, 75.410, 90.00, 90.00, 90.00
R / Rfree (%)	13.9 / 17.8

The binding sites of Copper atom in the Structure of Cu(I)Azurin at pH 6, with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Ctphpm" (pdb code 2ft7). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Structure of Cu(I)Azurin at pH 6, with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Ctphpm", PDB code: 2ft7:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in the Structure of Cu(I)Azurin at pH 6, with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Ctphpm"


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Cu(I)Azurin at pH 6, with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Ctphpm" within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu200 b:14.8 occ:0.50 CU A:CU1200 0.0 14.8 0.5 CU A:CU1200 0.9 18.4 0.5 ND1 A:HIS46 2.0 12.7 1.0 SG A:CYS112 2.2 11.8 1.0 SD A:MET117 2.6 14.9 1.0 ND1 A:HIS115 2.7 15.2 0.5 CE1 A:HIS46 2.9 12.8 1.0 CG A:HIS46 3.0 10.3 1.0 CB A:CYS112 3.0 10.4 1.0 CD2 A:HIS115 3.2 12.8 0.5 CE A:MET117 3.4 12.8 1.0 CB A:HIS46 3.5 10.2 1.0 CG A:HIS115 3.5 16.7 0.5 CB A:HIS115 3.5 15.7 0.5 CB A:HIS115 3.6 14.6 0.5 CA A:HIS46 3.6 11.7 1.0 CG A:HIS115 3.7 14.1 0.5 CE1 A:HIS115 3.7 16.8 0.5 O A:GLY45 3.8 14.9 1.0 NE2 A:HIS46 4.0 12.7 1.0 CD2 A:HIS46 4.1 11.3 1.0 CG A:MET117 4.2 19.4 1.0 NE2 A:HIS115 4.4 12.7 0.5 CA A:CYS112 4.5 9.8 1.0 N A:HIS115 4.5 16.0 0.5 N A:HIS46 4.5 11.5 1.0 C A:GLY45 4.5 13.9 1.0 CA A:HIS115 4.5 16.1 0.5 N A:HIS115 4.6 15.6 0.5 CA A:HIS115 4.6 15.8 0.5 N A:ASN47 4.6 9.4 1.0 C A:HIS46 4.7 8.9 1.0 CB A:MET117 4.7 16.3 1.0 O A:HIS115 4.7 15.0 0.5 CD2 A:HIS115 4.7 17.3 0.5 NE2 A:HIS115 4.8 20.1 0.5 CG A:PRO114 4.9 14.4 1.0 C A:HIS115 4.9 16.3 0.5 O A:ASN47 5.0 9.1 1.0

Copper binding site 2 out of 2 in the Structure of Cu(I)Azurin at pH 6, with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Ctphpm"


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Structure of Cu(I)Azurin at pH 6, with the Metal-Binding Loop Sequence "Ctfpghsalm" Replaced with "Ctphpm" within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu200 b:18.4 occ:0.50 CU A:CU1200 0.0 18.4 0.5 CU A:CU1200 0.9 14.8 0.5 SG A:CYS112 2.1 11.8 1.0 ND1 A:HIS46 2.1 12.7 1.0 ND1 A:HIS115 2.2 15.2 0.5 CD2 A:HIS115 2.5 12.8 0.5 O A:GLY45 3.0 14.9 1.0 CE1 A:HIS46 3.0 12.8 1.0 CG A:HIS46 3.1 10.3 1.0 CE1 A:HIS115 3.2 16.8 0.5 CG A:HIS115 3.2 16.7 0.5 CG A:HIS115 3.2 14.1 0.5 CA A:HIS46 3.3 11.7 1.0 SD A:MET117 3.3 14.9 1.0 CB A:CYS112 3.4 10.4 1.0 CB A:HIS115 3.4 14.6 0.5 CB A:HIS115 3.5 15.7 0.5 CB A:HIS46 3.5 10.2 1.0 NE2 A:HIS115 3.7 12.7 0.5 C A:GLY45 3.9 13.9 1.0 N A:HIS46 4.0 11.5 1.0 CG A:PRO114 4.1 14.4 1.0 N A:HIS115 4.2 16.0 0.5 NE2 A:HIS46 4.2 12.7 1.0 CE A:MET117 4.2 12.8 1.0 N A:HIS115 4.2 15.6 0.5 CD2 A:HIS46 4.3 11.3 1.0 NE2 A:HIS115 4.3 20.1 0.5 CD2 A:HIS115 4.3 17.3 0.5 N A:ASN47 4.4 9.4 1.0 C A:HIS46 4.4 8.9 1.0 CA A:HIS115 4.4 15.8 0.5 CA A:HIS115 4.4 16.1 0.5 ND1 A:HIS115 4.5 12.7 0.5 CE1 A:HIS115 4.7 10.1 0.5 CD A:PRO114 4.7 13.3 1.0 CA A:CYS112 4.7 9.8 1.0 O A:HIS115 4.9 15.0 0.5 CG A:MET117 4.9 19.4 1.0

C.Li, S.Yanagisawa, B.M.Martins, A.Messerschmidt, M.J.Banfield, C.Dennison. Basic Requirements For A Metal-Binding Site in A Protein: the Influence of Loop Shortening on the Cupredoxin Azurin. Proc.Natl.Acad.Sci.Usa V. 103 7258 2006.
ISSN: ISSN 0027-8424
PubMed: 16651527
DOI: 10.1073/PNAS.0600774103