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Sodium in PDB 1i2s: Beta-Lactamase From Bacillus Licheniformis BS3

Enzymatic activity of Beta-Lactamase From Bacillus Licheniformis BS3

All present enzymatic activity of Beta-Lactamase From Bacillus Licheniformis BS3:
3.5.2.6;

Protein crystallography data

The structure of Beta-Lactamase From Bacillus Licheniformis BS3, PDB code: 1i2s was solved by E.Fonze, M.Vanhove, G.Dive, E.Sauvage, J.M.Frere, P.Charlier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.362, 106.817, 63.901, 90.00, 94.43, 90.00
R / Rfree (%) 19.7 / 23.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Beta-Lactamase From Bacillus Licheniformis BS3 (pdb code 1i2s). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Beta-Lactamase From Bacillus Licheniformis BS3, PDB code: 1i2s:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 1i2s

Go back to Sodium Binding Sites List in 1i2s
Sodium binding site 1 out of 2 in the Beta-Lactamase From Bacillus Licheniformis BS3


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Beta-Lactamase From Bacillus Licheniformis BS3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1301

b:65.9
occ:1.00
O7 A:CIT1300 2.8 32.6 1.0
OH A:TYR274 2.9 23.9 1.0
C3 A:CIT1300 4.0 34.6 1.0
CZ A:TYR274 4.0 20.1 1.0
C4 A:CIT1300 4.2 41.2 1.0
CB A:ALA237 4.2 13.3 1.0
CE2 A:TYR274 4.2 19.3 1.0
C2 A:CIT1300 4.5 34.5 1.0
C5 A:CIT1300 4.7 46.0 1.0
O3 A:CIT1300 4.8 47.3 1.0

Sodium binding site 2 out of 2 in 1i2s

Go back to Sodium Binding Sites List in 1i2s
Sodium binding site 2 out of 2 in the Beta-Lactamase From Bacillus Licheniformis BS3


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Beta-Lactamase From Bacillus Licheniformis BS3 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na2301

b:71.2
occ:1.00
OH B:TYR274 2.8 24.0 1.0
O7 B:CIT2300 2.9 49.1 1.0
CB B:ALA237 3.8 15.4 1.0
CZ B:TYR274 3.8 21.3 1.0
CE2 B:TYR274 4.0 20.1 1.0
C3 B:CIT2300 4.1 48.6 1.0
C4 B:CIT2300 4.4 52.1 1.0
C2 B:CIT2300 4.7 47.1 1.0
O3 B:CIT2300 4.7 55.7 1.0
C5 B:CIT2300 4.7 54.8 1.0
NH1 B:ARG244 4.9 17.2 1.0

Reference:

E.Fonze, M.Vanhove, G.Dive, E.Sauvage, J.M.Frere, P.Charlier. Crystal Structures of the Bacillus Licheniformis BS3 Class A Beta-Lactamase and of the Acyl-Enzyme Adduct Formed with Cefoxitin Biochemistry V. 41 1877 2002.
ISSN: ISSN 0006-2960
PubMed: 11827533
DOI: 10.1021/BI015789K
Page generated: Sun Aug 17 05:16:30 2025

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