Atomistry » Copper » PDB 2fqd-2idf » 2i7o
Atomistry »
  Copper »
    PDB 2fqd-2idf »
      2i7o »

Copper in PDB 2i7o: Structure of Re(4,7-Dimethyl-Phen)(THR124HIS)(LYS122TRP)(HIS83GLN) Azcu(II), A Rhenium Modified Azurin Mutant

Protein crystallography data

The structure of Structure of Re(4,7-Dimethyl-Phen)(THR124HIS)(LYS122TRP)(HIS83GLN) Azcu(II), A Rhenium Modified Azurin Mutant, PDB code: 2i7o was solved by J.Sudhamsu, B.R.Crane, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.50
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 63.223, 69.075, 68.944, 90.00, 90.00, 90.00
R / Rfree (%) 23.6 / 25.5

Other elements in 2i7o:

The structure of Structure of Re(4,7-Dimethyl-Phen)(THR124HIS)(LYS122TRP)(HIS83GLN) Azcu(II), A Rhenium Modified Azurin Mutant also contains other interesting chemical elements:

Rhenium (Re) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the Structure of Re(4,7-Dimethyl-Phen)(THR124HIS)(LYS122TRP)(HIS83GLN) Azcu(II), A Rhenium Modified Azurin Mutant (pdb code 2i7o). 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(4,7-Dimethyl-Phen)(THR124HIS)(LYS122TRP)(HIS83GLN) Azcu(II), A Rhenium Modified Azurin Mutant, PDB code: 2i7o:

Copper binding site 1 out of 1 in 2i7o

Go back to Copper Binding Sites List in 2i7o
Copper binding site 1 out of 1 in the Structure of Re(4,7-Dimethyl-Phen)(THR124HIS)(LYS122TRP)(HIS83GLN) 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(4,7-Dimethyl-Phen)(THR124HIS)(LYS122TRP)(HIS83GLN) Azcu(II), A Rhenium Modified Azurin Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu901

b:16.2
occ:1.00
ND1 A:HIS46 2.0 14.6 1.0
ND1 A:HIS117 2.0 17.1 1.0
SG A:CYS112 2.2 18.4 1.0
CE1 A:HIS46 2.9 16.1 1.0
O A:GLY45 2.9 15.8 1.0
CE1 A:HIS117 3.0 16.2 1.0
CG A:HIS117 3.1 16.6 1.0
CG A:HIS46 3.1 15.7 1.0
SD A:MET121 3.2 15.5 1.0
CB A:CYS112 3.2 14.4 1.0
CB A:HIS117 3.4 16.7 1.0
CA A:HIS46 3.4 14.8 1.0
CB A:HIS46 3.6 14.8 1.0
CE A:MET121 3.8 16.0 1.0
CB A:PHE114 3.8 17.4 1.0
C A:GLY45 3.9 15.6 1.0
NE2 A:HIS46 4.1 15.6 1.0
N A:HIS46 4.1 15.3 1.0
NE2 A:HIS117 4.1 15.9 1.0
CD2 A:HIS117 4.2 17.6 1.0
CD2 A:HIS46 4.2 16.2 1.0
N A:ASN47 4.5 14.5 1.0
C A:HIS46 4.5 14.8 1.0
CA A:CYS112 4.6 13.4 1.0
CG A:PHE114 4.7 19.2 1.0
N A:PHE114 4.7 17.0 1.0
CG A:MET121 4.8 15.1 1.0
CA A:PHE114 4.9 17.8 1.0
CA A:HIS117 4.9 16.9 1.0

Reference:

C.Shih, A.K.Museth, M.Abrahamsson, A.M.Blanco-Rodriguez, A.J.Di Bilio, J.Sudhamsu, B.R.Crane, K.L.Ronayne, M.Towrie, A.Vlcek, J.H.Richards, J.R.Winkler, H.B.Gray. Tryptophan-Accelerated Electron Flow Through Proteins. Science V. 320 1760 2008.
ISSN: ISSN 0036-8075
PubMed: 18583608
DOI: 10.1126/SCIENCE.1158241
Page generated: Sun Dec 13 11:05:13 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy