Atomistry » Rhenium » PDB 1b0q-9ghx » 2i7o
Atomistry »
  Rhenium »
    PDB 1b0q-9ghx »
      2i7o »

Rhenium 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:

Copper (Cu) 1 atom

Rhenium Binding Sites:

The binding sites of Rhenium 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 Rhenium atom.
In total only one binding site of Rhenium was determined in the Structure of Re(4,7-Dimethyl-Phen)(THR124HIS)(LYS122TRP)(HIS83GLN) Azcu(II), A Rhenium Modified Azurin Mutant, PDB code: 2i7o:

Rhenium binding site 1 out of 1 in 2i7o

Go back to Rhenium Binding Sites List in 2i7o
Rhenium 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 Rhenium with other atoms in the Re 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:Re801

b:19.3
occ:1.00
RE A:REQ801 0.0 19.3 1.0
C3 A:REQ801 1.9 17.4 1.0
C2 A:REQ801 1.9 19.0 1.0
C1 A:REQ801 2.0 14.4 1.0
N1 A:REQ801 2.2 18.4 1.0
N2 A:REQ801 2.2 18.2 1.0
NE2 A:HIS124 2.2 16.1 1.0
C11 A:REQ801 3.0 18.0 1.0
C12 A:REQ801 3.0 18.3 1.0
O3 A:REQ801 3.0 16.8 1.0
O2 A:REQ801 3.1 19.3 1.0
O1 A:REQ801 3.1 22.5 1.0
CE1 A:HIS124 3.1 19.1 1.0
CD2 A:HIS124 3.2 17.5 1.0
C7 A:REQ801 3.2 18.2 1.0
C16 A:REQ801 3.2 19.9 1.0
ND1 A:HIS124 4.3 18.8 1.0
CG A:HIS124 4.3 17.4 1.0
C10 A:REQ801 4.4 17.9 1.0
C13 A:REQ801 4.4 19.3 1.0
C8 A:REQ801 4.5 18.7 1.0
C15 A:REQ801 4.5 20.4 1.0
SD A:MET109 4.7 19.1 1.0
CG A:GLN107 4.8 22.0 1.0
C9 A:REQ801 5.0 19.0 1.0
C14 A:REQ801 5.0 19.9 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: Thu Oct 10 12:23:31 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy