Magnesium in PDB 8k7q: Staphylococcus Aureus Lipase S116A Inactive Mutant-Psa Complex

All present enzymatic activity of Staphylococcus Aureus Lipase S116A Inactive Mutant-Psa Complex:
3.1.1.3;

The structure of Staphylococcus Aureus Lipase S116A Inactive Mutant-Psa Complex, PDB code: 8k7q was solved by J.Kitadokoro, S.Kamitani, K.Kitadokoro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.00 / 2.02
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	131.348, 131.348, 249.851, 90, 90, 90
R / Rfree (%)	21.8 / 23.9

The structure of Staphylococcus Aureus Lipase S116A Inactive Mutant-Psa Complex also contains other interesting chemical elements:

Zinc	(Zn)	2 atoms
Calcium	(Ca)	2 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Magnesium atom in the Staphylococcus Aureus Lipase S116A Inactive Mutant-Psa Complex (pdb code 8k7q). 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 Staphylococcus Aureus Lipase S116A Inactive Mutant-Psa Complex, PDB code: 8k7q:

Magnesium binding site 1 out of 1 in the Staphylococcus Aureus Lipase S116A Inactive Mutant-Psa Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Staphylococcus Aureus Lipase S116A Inactive Mutant-Psa Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg415 b:90.1 occ:1.00 O A:HOH553 2.4 62.9 1.0 O A:ASP23 2.8 82.1 1.0 O A:ASN201 3.4 72.0 1.0 CB A:ASN201 3.7 62.6 1.0 CG2 A:ILE202 3.9 60.1 1.0 C A:ASP23 4.0 78.0 1.0 C A:ASN201 4.1 64.5 1.0 O A:ALA25 4.3 66.4 1.0 CA A:ASN201 4.5 67.0 1.0 O A:HOH523 4.7 56.6 1.0 CA A:ASN24 4.7 52.5 1.0 N A:ASN24 4.8 59.6 1.0 N A:ILE202 4.9 57.6 1.0 C A:ASN24 4.9 51.2 1.0 CG A:ASN201 4.9 74.6 1.0

J.Kitadokoro, S.Kamitani, Y.Okuno, T.Hikima, M.Yamamoto, T.Hirokawa, K.Kitadokoro. Crystal Structure of Staphylococcus Aureus Lipase Complex with Unsaturated Petroselinic Acid. Febs Open Bio 2024.
ISSN: ESSN 2211-5463
PubMed: 38757397
DOI: 10.1002/2211-5463.13808