Atomistry » Magnesium » PDB 2uxj-2v7y » 2v4n
Atomistry »
  Magnesium »
    PDB 2uxj-2v7y »
      2v4n »

Magnesium in PDB 2v4n: Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form

Enzymatic activity of Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form

All present enzymatic activity of Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form:
3.1.3.5; 3.1.3.6; 3.6.1.11;

Protein crystallography data

The structure of Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form, PDB code: 2v4n was solved by P.Anju, H.S.Savithri, M.R.N.Murthy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 71.61 / 1.70
Space group F 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 73.730, 121.638, 143.256, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 21.2

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form (pdb code 2v4n). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form, PDB code: 2v4n:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2v4n

Go back to Magnesium Binding Sites List in 2v4n
Magnesium binding site 1 out of 2 in the Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1254

b:20.4
occ:1.00
OD1 A:ASP9 2.2 28.4 1.0
OD1 A:ASN92 2.3 22.1 1.0
OG A:SER39 2.5 22.5 1.0
O A:HOH2282 2.5 19.8 1.0
O A:HOH2113 2.6 24.9 1.0
OD2 A:ASP8 2.6 29.5 1.0
CG A:ASP9 3.2 26.5 1.0
CG A:ASP8 3.2 25.7 1.0
CG A:ASN92 3.2 22.9 1.0
OD1 A:ASP8 3.3 28.4 1.0
ND2 A:ASN92 3.5 21.6 1.0
CB A:SER39 3.5 22.5 1.0
OD2 A:ASP9 3.6 30.2 1.0
CA A:SER39 4.0 22.7 1.0
O A:HOH2051 4.0 29.1 1.0
O A:HOH2010 4.0 20.5 1.0
O A:HOH2045 4.3 35.1 1.0
N A:ASP9 4.3 23.5 1.0
O A:HOH2284 4.4 17.3 1.0
OG1 A:THR106 4.4 23.9 1.0
CB A:ASP9 4.4 24.4 1.0
CB A:ASP8 4.4 23.3 1.0
OD1 A:ASN37 4.5 25.6 1.0
CA A:ASP9 4.5 24.3 1.0
C A:ASP8 4.6 23.0 1.0
N A:SER39 4.6 22.3 1.0
CB A:ASN92 4.6 21.9 1.0
O A:ALA93 4.7 22.5 1.0
O3 A:PO41257 4.8 14.1 0.5
CA A:ASP8 5.0 23.0 1.0

Magnesium binding site 2 out of 2 in 2v4n

Go back to Magnesium Binding Sites List in 2v4n
Magnesium binding site 2 out of 2 in the Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Salmonella Typhimurium Sure at 1.7 Angstrom Resolution in Orthorhombic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1255

b:21.8
occ:0.50
O A:GLY248 2.2 19.9 1.0
O A:THR251 2.6 20.9 1.0
O A:HOH2277 3.3 35.0 1.0
C A:GLY248 3.4 20.0 1.0
C A:THR251 3.8 20.9 1.0
CA A:GLY248 4.0 20.1 1.0
CA A:GLN252 4.3 20.4 1.0
N A:VAL249 4.4 20.1 1.0
N A:GLN252 4.5 20.1 1.0
C A:GLN252 4.6 20.4 1.0
N A:THR251 4.6 21.3 1.0
O A:GLN252 4.7 20.1 1.0
CA A:VAL249 4.7 20.7 1.0
CA A:THR251 4.8 21.1 1.0
N A:GLY250 5.0 21.0 1.0

Reference:

A.Pappachan, H.S.Savithri, M.R.N.Murthy. Structural and Functional Studies on A Mesophilic Stationary Phase Survival Protein (Sur E) From Salmonella Typhimurium Febs J. V. 275 5855 2008.
ISSN: ISSN 1742-464X
PubMed: 19021761
DOI: 10.1111/J.1742-4658.2008.06715.X
Page generated: Wed Aug 14 04:57:49 2024

Last articles

Mg in 1RYH
Mg in 1RYF
Mg in 1RY5
Mg in 1RYA
Mg in 1RVJ
Mg in 1RVC
Mg in 1RVK
Mg in 1RU1
Mg in 1RVD
Mg in 1RTZ
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy