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Magnesium in PDB 6mod: Co-Crystal Structure of P. Aeruginosa Lpxc-50432 Complex

Enzymatic activity of Co-Crystal Structure of P. Aeruginosa Lpxc-50432 Complex

All present enzymatic activity of Co-Crystal Structure of P. Aeruginosa Lpxc-50432 Complex:
3.5.1.108;

Protein crystallography data

The structure of Co-Crystal Structure of P. Aeruginosa Lpxc-50432 Complex, PDB code: 6mod was solved by A.J.Stein, M.C.Holt, Z.Assar, 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) 63.45 / 1.85
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 36.079, 66.911, 63.462, 90.00, 91.08, 90.00
R / Rfree (%) 18.4 / 23.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Co-Crystal Structure of P. Aeruginosa Lpxc-50432 Complex (pdb code 6mod). 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-50432 Complex, PDB code: 6mod:

Magnesium binding site 1 out of 1 in 6mod

Go back to Magnesium Binding Sites List in 6mod
Magnesium binding site 1 out of 1 in the Co-Crystal Structure of P. Aeruginosa Lpxc-50432 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-50432 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg301

b:14.4
occ:1.00
OD1 A:ASP241 2.1 19.2 1.0
O6 A:JWV302 2.2 23.4 1.0
NE2 A:HIS78 2.2 21.5 1.0
NE2 A:HIS237 2.2 17.7 1.0
O7 A:JWV302 2.3 22.6 1.0
OD2 A:ASP241 2.5 20.3 1.0
CG A:ASP241 2.6 19.6 1.0
C19 A:JWV302 2.9 23.4 1.0
N2 A:JWV302 3.0 23.6 1.0
CE1 A:HIS237 3.1 16.8 1.0
CD2 A:HIS78 3.1 21.0 1.0
CD2 A:HIS237 3.2 17.2 1.0
CE1 A:HIS78 3.2 22.6 1.0
OG1 A:THR190 4.1 20.9 1.0
CB A:ASP241 4.1 18.1 1.0
ND1 A:HIS237 4.2 17.4 1.0
CG A:GLU77 4.2 20.5 1.0
CG A:HIS78 4.3 20.9 1.0
CG A:HIS237 4.3 17.1 1.0
OE2 A:GLU77 4.3 25.9 1.0
ND1 A:HIS78 4.3 22.4 1.0
C14 A:JWV302 4.3 23.1 1.0
CB A:THR190 4.4 21.6 1.0
C16 A:JWV302 4.5 24.6 1.0
O4 A:JWV302 4.6 24.9 1.0
C17 A:JWV302 4.7 25.0 1.0
CE1 A:HIS264 4.8 27.5 1.0
CD A:GLU77 4.8 23.4 1.0
CA A:ASP241 4.8 19.3 1.0
C15 A:JWV302 4.9 24.0 1.0
NE2 A:HIS264 4.9 27.7 1.0
N1 A:JWV302 4.9 21.5 1.0
O A:HIS237 4.9 18.8 1.0
CA A:THR190 5.0 21.6 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 11:56:00 2024

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