Copper in PDB 4k9j: Structure of Re(Co)3(4,7-Dimethyl-Phen)(THR126HIS)(LYS122TRP) (HIS83GLU)(TRP48PHE)(TYR72PHE)(TYR108PHE)Azcu(II), A Rhenium Modified Azurin Mutant

The structure of Structure of Re(Co)3(4,7-Dimethyl-Phen)(THR126HIS)(LYS122TRP) (HIS83GLU)(TRP48PHE)(TYR72PHE)(TYR108PHE)Azcu(II), A Rhenium Modified Azurin Mutant, PDB code: 4k9j was solved by K.Takematsu, H.R.Williamson, A.M.Blanco-Rodriguez, L.Sokolova, P.Nikolovski, J.T.Kaiser, M.Towrie, I.P.Clark, A.Vlcek Jr, J.R.Winkler, H.B.Gray, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.35 / 1.70
Space group	F 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	42.391, 93.215, 109.383, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 23.6

The structure of Structure of Re(Co)3(4,7-Dimethyl-Phen)(THR126HIS)(LYS122TRP) (HIS83GLU)(TRP48PHE)(TYR72PHE)(TYR108PHE)Azcu(II), A Rhenium Modified Azurin Mutant also contains other interesting chemical elements:

Rhenium

(Re)

1 atom

The binding sites of Copper atom in the Structure of Re(Co)3(4,7-Dimethyl-Phen)(THR126HIS)(LYS122TRP) (HIS83GLU)(TRP48PHE)(TYR72PHE)(TYR108PHE)Azcu(II), A Rhenium Modified Azurin Mutant (pdb code 4k9j). 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 Re(Co)3(4,7-Dimethyl-Phen)(THR126HIS)(LYS122TRP) (HIS83GLU)(TRP48PHE)(TYR72PHE)(TYR108PHE)Azcu(II), A Rhenium Modified Azurin Mutant, PDB code: 4k9j:

Copper binding site 1 out of 1 in the Structure of Re(Co)3(4,7-Dimethyl-Phen)(THR126HIS)(LYS122TRP) (HIS83GLU)(TRP48PHE)(TYR72PHE)(TYR108PHE)Azcu(II), A Rhenium Modified Azurin Mutant


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of Re(Co)3(4,7-Dimethyl-Phen)(THR126HIS)(LYS122TRP) (HIS83GLU)(TRP48PHE)(TYR72PHE)(TYR108PHE)Azcu(II), A Rhenium Modified Azurin Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cu201 b:30.4 occ:1.00 ND1 A:HIS117 2.0 16.7 1.0 ND1 A:HIS46 2.1 16.5 1.0 SG A:CYS112 2.3 16.4 1.0 HA A:HIS46 2.7 17.3 1.0 CE1 A:HIS117 2.9 17.4 1.0 O A:GLY45 2.9 17.5 1.0 CE1 A:HIS46 3.0 17.6 1.0 SD A:MET121 3.0 16.7 1.0 HE1 A:HIS117 3.0 20.8 1.0 HE1 A:HIS46 3.1 21.1 1.0 CG A:HIS117 3.1 18.2 1.0 HB3 A:PHE114 3.1 24.8 1.0 HB3 A:HIS117 3.1 21.9 1.0 CG A:HIS46 3.2 15.1 1.0 HB3 A:CYS112 3.2 18.2 1.0 CB A:CYS112 3.3 15.2 1.0 HE3 A:MET121 3.3 17.9 1.0 CB A:HIS117 3.5 18.3 1.0 HB2 A:CYS112 3.5 18.2 1.0 HB3 A:HIS46 3.5 16.7 1.0 CA A:HIS46 3.5 14.4 1.0 HB2 A:HIS117 3.5 21.9 1.0 HB2 A:PHE114 3.6 24.8 1.0 CB A:HIS46 3.6 13.9 1.0 CE A:MET121 3.6 14.9 1.0 CB A:PHE114 3.8 20.7 1.0 HE1 A:MET121 3.8 17.9 1.0 C A:GLY45 3.9 16.9 1.0 H A:ASN47 4.0 19.0 1.0 NE2 A:HIS117 4.0 19.2 1.0 H A:PHE114 4.1 23.9 1.0 NE2 A:HIS46 4.1 17.0 1.0 CD2 A:HIS117 4.2 19.8 1.0 N A:HIS46 4.2 15.6 1.0 CD2 A:HIS46 4.3 15.5 1.0 CG A:MET121 4.5 16.9 1.0 HE2 A:MET121 4.5 17.9 1.0 HB2 A:HIS46 4.5 16.7 1.0 N A:ASN47 4.6 15.9 1.0 HB2 A:MET121 4.6 20.3 1.0 C A:HIS46 4.6 13.4 1.0 CG A:PHE114 4.6 21.8 1.0 CA A:CYS112 4.7 15.4 1.0 N A:PHE114 4.7 19.9 1.0 HG3 A:MET121 4.8 20.3 1.0 HG3 A:MET13 4.8 31.0 1.0 HB3 A:MET121 4.8 20.3 1.0 HE2 A:HIS117 4.8 23.0 1.0 CA A:PHE114 4.9 21.0 1.0 HE2 A:HIS46 4.9 20.4 1.0 HD1 A:PHE114 4.9 26.6 1.0 CB A:MET121 4.9 16.9 1.0 CA A:HIS117 4.9 20.3 1.0 H A:HIS46 5.0 18.7 1.0

K.Takematsu, H.Williamson, A.M.Blanco-Rodriguez, L.Sokolova, P.Nikolovski, J.T.Kaiser, M.Towrie, I.P.Clark, A.Vlcek, J.R.Winkler, H.B.Gray. Tryptophan-Accelerated Electron Flow Across A Protein-Protein Interface. J.Am.Chem.Soc. V. 135 15515 2013.
ISSN: ISSN 0002-7863
PubMed: 24032375
DOI: 10.1021/JA406830D