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Cadmium in PDB 5haq: Oxa-48 Beta-Lactamase Mutant - S70G

Enzymatic activity of Oxa-48 Beta-Lactamase Mutant - S70G

All present enzymatic activity of Oxa-48 Beta-Lactamase Mutant - S70G:
3.5.2.6;

Protein crystallography data

The structure of Oxa-48 Beta-Lactamase Mutant - S70G, PDB code: 5haq was solved by V.Stojanoski, C.J.Adamski, L.Hu, S.C.Mehta, B.Sankaran, B.V.V.Prasad, T.G.Palzkill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 60.00 / 2.14
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.660, 73.611, 106.360, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / 21.1

Cadmium Binding Sites:

The binding sites of Cadmium atom in the Oxa-48 Beta-Lactamase Mutant - S70G (pdb code 5haq). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 4 binding sites of Cadmium where determined in the Oxa-48 Beta-Lactamase Mutant - S70G, PDB code: 5haq:
Jump to Cadmium binding site number: 1; 2; 3; 4;

Cadmium binding site 1 out of 4 in 5haq

Go back to Cadmium Binding Sites List in 5haq
Cadmium binding site 1 out of 4 in the Oxa-48 Beta-Lactamase Mutant - S70G


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Oxa-48 Beta-Lactamase Mutant - S70G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd301

b:32.6
occ:1.00
CE1 A:HIS38 2.5 25.6 1.0
OE1 A:GLU256 2.6 29.4 1.0
OE2 A:GLU256 2.6 28.2 1.0
OE1 A:GLU37 2.8 46.2 1.0
CD A:GLU256 2.9 30.0 1.0
NE2 A:HIS38 3.0 26.2 1.0
CD A:CD302 3.3 38.3 1.0
ND1 A:HIS38 3.6 31.8 1.0
CD A:GLU37 3.9 48.5 1.0
CD2 A:HIS38 4.2 26.1 1.0
CG A:GLU256 4.4 27.2 1.0
CG A:HIS38 4.5 30.1 1.0
OE2 A:GLU37 4.5 55.5 1.0
CB A:GLU37 4.5 42.9 1.0
CG A:GLU37 4.9 51.0 1.0
O A:HIS34 4.9 32.7 1.0

Cadmium binding site 2 out of 4 in 5haq

Go back to Cadmium Binding Sites List in 5haq
Cadmium binding site 2 out of 4 in the Oxa-48 Beta-Lactamase Mutant - S70G


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Oxa-48 Beta-Lactamase Mutant - S70G within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd302

b:38.3
occ:1.00
ND1 A:HIS34 2.5 31.2 1.0
OE1 A:GLU37 2.6 46.2 1.0
OE2 A:GLU256 2.7 28.2 1.0
OE2 A:GLU37 3.1 55.5 1.0
CD A:GLU37 3.2 48.5 1.0
CD A:CD301 3.3 32.6 1.0
CE1 A:HIS34 3.3 32.5 1.0
CD A:GLU256 3.5 30.0 1.0
CG A:HIS34 3.6 30.1 1.0
CB A:HIS34 4.0 29.4 1.0
CB A:GLU256 4.1 26.6 1.0
CA A:HIS34 4.1 31.7 1.0
OE1 A:GLU256 4.1 29.4 1.0
CG A:GLU256 4.2 27.2 1.0
NE2 A:HIS34 4.5 35.2 1.0
CG A:GLU37 4.6 51.0 1.0
CD2 A:HIS34 4.7 33.1 1.0
O A:HOH417 4.8 34.4 1.0
N A:HIS34 4.8 31.1 1.0

Cadmium binding site 3 out of 4 in 5haq

Go back to Cadmium Binding Sites List in 5haq
Cadmium binding site 3 out of 4 in the Oxa-48 Beta-Lactamase Mutant - S70G


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of Oxa-48 Beta-Lactamase Mutant - S70G within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cd301

b:36.4
occ:1.00
OD2 B:ASP143 2.5 37.3 1.0
OD1 B:ASP143 2.6 38.0 1.0
CG B:ASP143 2.9 35.5 1.0
CB B:ASP143 4.3 33.2 1.0
O B:HIS140 4.6 31.9 1.0
O B:ALA141 4.6 30.0 1.0

Cadmium binding site 4 out of 4 in 5haq

Go back to Cadmium Binding Sites List in 5haq
Cadmium binding site 4 out of 4 in the Oxa-48 Beta-Lactamase Mutant - S70G


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 4 of Oxa-48 Beta-Lactamase Mutant - S70G within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cd302

b:43.0
occ:1.00
O B:HOH449 2.4 52.6 1.0
OE1 B:GLU147 2.6 38.7 1.0
OE2 B:GLU147 2.7 34.7 1.0
CD B:GLU147 3.0 33.2 1.0
CD2 B:HIS140 3.7 41.2 1.0
OD1 B:ASP143 4.1 38.0 1.0
O B:HIS140 4.3 31.9 1.0
CG B:GLU147 4.4 35.3 1.0
CG B:HIS140 4.5 39.1 1.0
NE2 B:HIS140 4.7 46.4 1.0
CA B:HIS140 4.7 33.2 1.0
CB B:HIS140 4.7 31.8 1.0
C B:HIS140 5.0 31.5 1.0

Reference:

V.Stojanoski, C.J.Adamski, L.Hu, S.C.Mehta, B.Sankaran, P.Zwart, B.V.Prasad, T.Palzkill. Removal of the Side Chain at the Active-Site Serine By A Glycine Substitution Increases the Stability of A Wide Range of Serine Beta-Lactamases By Relieving Steric Strain. Biochemistry V. 55 2479 2016.
ISSN: ISSN 0006-2960
PubMed: 27073009
DOI: 10.1021/ACS.BIOCHEM.6B00056
Page generated: Fri Jul 19 18:28:07 2024

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