Magnesium in PDB 8us3: C2 Crystal Structure of Tama From Pseudomonas Aeruginosa at 3.1 Ang

Protein crystallography data

The structure of C2 Crystal Structure of Tama From Pseudomonas Aeruginosa at 3.1 Ang, PDB code: 8us3 was solved by A.Mellouk, T.F.Moraes, C.Calmettes, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.60 / 3.10
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 140.4, 63.88, 81.36, 90, 99.4, 90
R / Rfree (%) 25 / 30

Magnesium Binding Sites:

The binding sites of Magnesium atom in the C2 Crystal Structure of Tama From Pseudomonas Aeruginosa at 3.1 Ang (pdb code 8us3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the C2 Crystal Structure of Tama From Pseudomonas Aeruginosa at 3.1 Ang, PDB code: 8us3:

Magnesium binding site 1 out of 1 in 8us3

Go back to Magnesium Binding Sites List in 8us3
Magnesium binding site 1 out of 1 in the C2 Crystal Structure of Tama From Pseudomonas Aeruginosa at 3.1 Ang


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of C2 Crystal Structure of Tama From Pseudomonas Aeruginosa at 3.1 Ang within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg602

b:59.0
occ:1.00
O A:ILE203 3.3 91.6 1.0
CD1 A:LEU208 3.5 93.0 1.0
O A:SER201 3.8 139.6 1.0
CG A:GLU205 4.0 123.5 1.0
OE2 A:GLU205 4.1 125.7 1.0
CB A:PHE197 4.4 99.9 1.0
CD A:GLU205 4.5 127.9 1.0
C A:ILE203 4.5 99.9 1.0
C A:SER201 4.7 152.5 1.0
O A:PHE197 4.7 124.5 1.0
CB A:SER201 4.8 135.2 1.0
CG A:LEU208 4.9 92.2 1.0
N A:GLU205 5.0 126.1 1.0

Reference:

A.Mellouk, P.L.Jaouen, L.J.Ruel, M.Le, C.Martini, T.F.Moraes, M.El Bakkouri, P.Lague, E.Boisselier, C.Calmettes. Potra Domains of the Tama Insertase Interact with the Outer Membrane and Modulate Membrane Properties Proc.Natl.Acad.Sci.Usa 2024.
ISSN: ESSN 1091-6490
DOI: 10.1073/PNAS.2402543121
Page generated: Fri Oct 4 21:25:58 2024

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