Atomistry » Magnesium » PDB 2c42-2cic » 2c4r
Atomistry »
  Magnesium »
    PDB 2c42-2cic »
      2c4r »

Magnesium in PDB 2c4r: Catalytic Domain of E. Coli Rnase E

Protein crystallography data

The structure of Catalytic Domain of E. Coli Rnase E, PDB code: 2c4r was solved by M.J.Marcaida, A.J.Callaghan, B.F.Luisi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 3.60
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 196.586, 196.586, 140.766, 90.00, 90.00, 120.00
R / Rfree (%) 31.9 / 34.7

Other elements in 2c4r:

The structure of Catalytic Domain of E. Coli Rnase E also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Catalytic Domain of E. Coli Rnase E (pdb code 2c4r). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Catalytic Domain of E. Coli Rnase E, PDB code: 2c4r:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2c4r

Go back to Magnesium Binding Sites List in 2c4r
Magnesium binding site 1 out of 2 in the Catalytic Domain of E. Coli Rnase E


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catalytic Domain of E. Coli Rnase E within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Mg1510

b:48.1
occ:0.50
O L:THR410 3.8 60.0 1.0
C L:THR410 4.5 66.3 1.0
O L:SER295 4.6 59.0 1.0
O L:GLY409 4.7 84.0 1.0
OD1 L:ASP294 4.8 70.8 1.0
CA L:THR410 4.9 68.3 1.0

Magnesium binding site 2 out of 2 in 2c4r

Go back to Magnesium Binding Sites List in 2c4r
Magnesium binding site 2 out of 2 in the Catalytic Domain of E. Coli Rnase E


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Catalytic Domain of E. Coli Rnase E within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Mg1511

b:52.1
occ:1.00
O L:HOH2004 2.2 50.3 1.0
O L:HOH2001 2.2 52.6 1.0
O L:HOH2003 2.2 44.5 1.0
O L:HOH2002 2.2 49.6 1.0
O L:HOH2005 2.2 50.5 1.0
OD2 L:ASP346 2.6 66.7 1.0
OD2 L:ASP303 2.8 60.4 1.0
O L:ILE304 3.7 42.8 1.0
CG L:ASP346 3.8 62.5 1.0
CG L:ASP303 3.9 60.2 1.0
OD1 L:ASP303 4.3 65.0 1.0
OD1 L:ASP346 4.4 64.9 1.0
O L:ASP346 4.6 51.5 1.0
C L:ILE304 4.9 42.0 1.0
CB L:ASP346 4.9 56.6 1.0
CD1 L:ILE348 5.0 43.8 1.0

Reference:

A.J.Callaghan, M.J.Marcaida, J.A.Stead, K.J.Mcdowall, W.G.Scott, B.F.Luisi. Structure of E. Coli Rnase E Catalytic Domain and Implications For Rna Processing and Turnover Nature V. 437 1187 2005.
ISSN: ISSN 0028-0836
PubMed: 16237448
DOI: 10.1038/NATURE04084
Page generated: Mon Dec 14 07:18:29 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