Magnesium in PDB 2qin: Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant

All present enzymatic activity of Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant:
3.5.2.6;

The structure of Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant, PDB code: 2qin was solved by J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.84 / 1.76
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	66.141, 112.845, 78.352, 90.00, 113.35, 90.00
R / Rfree (%)	17.3 / 21.2

The structure of Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant also contains other interesting chemical elements:

Zinc

(Zn)

9 atoms

The binding sites of Magnesium atom in the Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant (pdb code 2qin). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant, PDB code: 2qin:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg4001 b:23.9 occ:1.00 O D:HOH4031 2.1 21.9 1.0 O D:HOH4120 2.1 24.5 1.0 O D:HOH4242 2.1 29.1 1.0 O D:HOH4366 2.2 28.4 1.0 O D:HOH4130 2.2 25.3 1.0 O D:HOH4259 2.3 25.2 1.0 O D:HOH4103 4.1 27.2 1.0 OD2 D:ASP108 4.1 14.0 1.0 O D:HOH4094 4.3 23.2 1.0 OD1 D:ASP108 4.4 14.9 1.0 O D:HOH4161 4.4 35.3 1.0 CG D:ASP108 4.7 14.4 1.0

Magnesium binding site 2 out of 2 in the Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Stenotrophomonas Maltophilia L1 Metallo-Beta-Lactamase Asp-120 Cys Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg4002 b:17.8 occ:1.00 O B:HOH4068 2.0 20.0 1.0 O B:HOH4350 2.0 22.9 1.0 O B:HOH4046 2.0 19.1 1.0 O B:HOH4110 2.0 18.4 1.0 O B:HOH4098 2.2 17.7 1.0 O B:HOH4090 2.2 20.5 1.0 O B:HOH4042 3.9 22.1 1.0 OD2 B:ASP67 4.1 16.4 1.0 OD1 B:ASP270 4.2 15.0 1.0 OD1 B:ASP67 4.2 16.0 1.0 O B:HOH4128 4.3 33.1 1.0 CG B:ASP67 4.5 14.4 1.0 O B:HOH4099 4.6 27.1 1.0 CG B:ASP270 4.9 14.2 1.0

J.Crisp, R.Conners, J.D.Garrity, A.L.Carenbauer, M.W.Crowder, J.Spencer. Structural Basis For the Role of Asp-120 in Metallo-Beta-Lactamases. Biochemistry V. 46 10664 2007.
ISSN: ISSN 0006-2960
PubMed: 17715946
DOI: 10.1021/BI700707U