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Magnesium in PDB 6mo4: Co-Crystal Structure of P. Aeruginosa Lpxc-50067 Complex

Enzymatic activity of Co-Crystal Structure of P. Aeruginosa Lpxc-50067 Complex

All present enzymatic activity of Co-Crystal Structure of P. Aeruginosa Lpxc-50067 Complex:
3.5.1.108;

Protein crystallography data

The structure of Co-Crystal Structure of P. Aeruginosa Lpxc-50067 Complex, PDB code: 6mo4 was solved by A.J.Stein, Z.Assar, M.C.Holt, F.Cohen, L.Andrews, R.Cirz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.36 / 1.84
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 36.125, 66.717, 63.655, 90.00, 90.72, 90.00
R / Rfree (%) 17.7 / 22.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Co-Crystal Structure of P. Aeruginosa Lpxc-50067 Complex (pdb code 6mo4). 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 Co-Crystal Structure of P. Aeruginosa Lpxc-50067 Complex, PDB code: 6mo4:

Magnesium binding site 1 out of 1 in 6mo4

Go back to Magnesium Binding Sites List in 6mo4
Magnesium binding site 1 out of 1 in the Co-Crystal Structure of P. Aeruginosa Lpxc-50067 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Co-Crystal Structure of P. Aeruginosa Lpxc-50067 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:11.9
occ:1.00
NE2 A:HIS237 2.1 12.1 1.0
O4 A:JWM302 2.1 18.4 1.0
OD1 A:ASP241 2.1 14.4 1.0
NE2 A:HIS78 2.2 14.0 1.0
O5 A:JWM302 2.3 16.9 1.0
OD2 A:ASP241 2.4 12.3 1.0
CG A:ASP241 2.6 15.2 1.0
C18 A:JWM302 2.8 21.5 1.0
N1 A:JWM302 2.9 19.4 1.0
CE1 A:HIS237 3.0 13.0 1.0
CD2 A:HIS78 3.1 14.7 1.0
CD2 A:HIS237 3.1 10.6 1.0
CE1 A:HIS78 3.2 19.2 1.0
CB A:ASP241 4.1 13.4 1.0
OG1 A:THR190 4.1 16.9 1.0
ND1 A:HIS237 4.1 12.9 1.0
CG A:HIS237 4.2 13.5 1.0
CG A:HIS78 4.3 16.9 1.0
ND1 A:HIS78 4.3 20.2 1.0
C13 A:JWM302 4.3 19.4 1.0
CB A:THR190 4.3 15.0 1.0
CG A:GLU77 4.3 20.0 1.0
OE2 A:GLU77 4.4 22.1 1.0
C16 A:JWM302 4.6 23.9 1.0
CE1 A:HIS264 4.8 22.3 1.0
CA A:ASP241 4.8 12.9 1.0
C14 A:JWM302 4.8 23.0 1.0
CD A:GLU77 4.9 20.0 1.0
N A:JWM302 4.9 18.7 1.0
C15 A:JWM302 4.9 24.3 1.0
O A:HIS237 4.9 14.8 1.0
CA A:THR190 4.9 14.4 1.0
NE2 A:HIS264 5.0 26.3 1.0

Reference:

F.Cohen, J.B.Aggen, L.D.Andrews, Z.Assar, J.Boggs, T.Choi, P.Dozzo, A.N.Easterday, C.M.Haglund, D.J.Hildebrandt, M.C.Holt, K.Joly, A.Jubb, Z.Kamal, T.R.Kane, A.W.Konradi, K.M.Krause, M.S.Linsell, T.D.Machajewski, O.Miroshnikova, H.E.Moser, V.Nieto, T.Phan, C.Plato, A.W.Serio, J.Seroogy, A.Shakhmin, A.J.Stein, A.D.Sun, S.Sviridov, Z.Wang, K.Wlasichuk, W.Yang, X.Zhou, H.Zhu, R.T.Cirz. Optimization of Lpxc Inhibitors For Antibacterial Activity and Cardiovascular Safety. Chemmedchem V. 14 1560 2019.
ISSN: ESSN 1860-7187
PubMed: 31283109
DOI: 10.1002/CMDC.201900287
Page generated: Tue Oct 1 11:55:29 2024

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