Atomistry » Copper » PDB 1oe2-1rjp » 1q05
Atomistry »
  Copper »
    PDB 1oe2-1rjp »
      1q05 »

Copper in PDB 1q05: Crystal Structure of the Cu(I) Form of E. Coli Cuer, A Copper Efflux Regulator

Protein crystallography data

The structure of Crystal Structure of the Cu(I) Form of E. Coli Cuer, A Copper Efflux Regulator, PDB code: 1q05 was solved by A.Changela, K.Chen, Y.Xue, J.Holschen, C.E.Outten, T.V.O'halloran, A.Mondragon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.92 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 59.160, 66.260, 81.290, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 25.3

Copper Binding Sites:

The binding sites of Copper atom in the Crystal Structure of the Cu(I) Form of E. Coli Cuer, A Copper Efflux Regulator (pdb code 1q05). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total 2 binding sites of Copper where determined in the Crystal Structure of the Cu(I) Form of E. Coli Cuer, A Copper Efflux Regulator, PDB code: 1q05:
Jump to Copper binding site number: 1; 2;

Copper binding site 1 out of 2 in 1q05

Go back to Copper Binding Sites List in 1q05
Copper binding site 1 out of 2 in the Crystal Structure of the Cu(I) Form of E. Coli Cuer, A Copper Efflux Regulator


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Crystal Structure of the Cu(I) Form of E. Coli Cuer, A Copper Efflux Regulator within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu302

b:40.7
occ:1.00
SG A:CYS120 2.2 38.5 1.0
SG A:CYS112 2.2 47.0 1.0
CB A:CYS120 3.1 39.5 1.0
CB A:CYS112 3.1 53.2 1.0
CA A:CYS120 3.3 39.1 1.0
O B:SER77 3.5 54.3 1.0
CD1 A:ILE122 3.6 37.8 1.0
CG1 A:ILE122 3.6 38.4 1.0
CD A:PRO121 3.7 38.5 1.0
C A:CYS120 3.8 38.2 1.0
N A:PRO121 3.8 38.5 1.0
CA B:SER77 4.0 56.0 1.0
N A:ILE122 4.0 37.6 1.0
CB A:ILE122 4.1 37.8 1.0
C B:SER77 4.2 54.9 1.0
CA A:CYS112 4.2 55.4 1.0
CB B:SER77 4.3 56.1 1.0
OG B:SER77 4.5 58.3 1.0
CB B:VAL80 4.6 45.6 1.0
N A:CYS120 4.7 39.6 1.0
CA A:ILE122 4.7 38.0 1.0
O A:CYS120 4.7 37.8 1.0
N B:LYS81 4.7 45.6 1.0
CG1 B:VAL80 4.7 44.1 1.0
CB B:LYS81 4.8 46.7 1.0
CD A:PRO113 4.9 59.5 1.0
CA A:PRO121 4.9 38.0 1.0
C A:CYS112 4.9 57.0 1.0
N A:GLY114 4.9 61.1 1.0
C A:PRO121 5.0 38.1 1.0

Copper binding site 2 out of 2 in 1q05

Go back to Copper Binding Sites List in 1q05
Copper binding site 2 out of 2 in the Crystal Structure of the Cu(I) Form of E. Coli Cuer, A Copper Efflux Regulator


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 2 of Crystal Structure of the Cu(I) Form of E. Coli Cuer, A Copper Efflux Regulator within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cu301

b:26.4
occ:1.00
SG B:CYS112 2.1 24.5 1.0
SG B:CYS120 2.1 29.8 1.0
CB B:CYS120 3.1 30.4 1.0
CB B:CYS112 3.2 24.8 1.0
CB A:SER77 3.4 27.4 1.0
CA B:CYS120 3.5 31.5 1.0
O A:SER77 3.6 28.1 1.0
CG1 B:ILE122 3.7 28.3 1.0
CD1 B:ILE122 3.7 26.7 1.0
CD B:PRO121 3.8 28.7 1.0
CA A:SER77 3.9 28.4 1.0
C B:CYS120 4.0 31.7 1.0
N B:PRO121 4.1 29.9 1.0
CA B:CYS112 4.1 27.0 1.0
CB B:ILE122 4.1 28.4 1.0
C A:SER77 4.1 29.1 1.0
N B:ILE122 4.2 28.7 1.0
CB A:VAL80 4.3 28.0 1.0
OG A:SER77 4.4 27.9 1.0
CD B:PRO113 4.5 28.6 1.0
CG B:PRO121 4.5 32.5 1.0
N A:LYS81 4.6 24.6 1.0
CG1 A:VAL80 4.7 28.0 1.0
O B:ASP119 4.7 36.5 1.0
N B:CYS120 4.8 34.4 1.0
CA B:ILE122 4.8 27.9 1.0
O B:CYS120 4.8 32.9 1.0
CB A:LYS81 4.9 24.6 1.0
C B:CYS112 4.9 28.8 1.0
N B:PRO113 4.9 29.5 1.0
CG2 A:VAL80 5.0 28.2 1.0

Reference:

A.Changela, K.Chen, Y.Xue, J.Holschen, C.E.Outten, T.V.O'halloran, A.Mondragon. Molecular Basis of Metal-Ion Selectivity and Zeptomolar Sensitivity By Cuer Science V. 301 1383 2003.
ISSN: ISSN 0036-8075
PubMed: 12958362
DOI: 10.1126/SCIENCE.1085950
Page generated: Sun Dec 13 11:01:29 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy