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Cadmium in PDB 6cac: Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop
Enzymatic activity of Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop
All present enzymatic activity of Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop:
3.5.2.6;
3.5.2.6;
Protein crystallography data
The structure of Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop, PDB code: 6cac
was solved by
P.M.Alzari,
E.Giannini,
A.Palacios,
M.Mojica,
R.Bonomo,
L.Llarrull,
A.Vila,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 45.87 / 1.79 |
| Space group | C 1 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 91.707, 91.737, 134.329, 90.00, 107.16, 90.00 |
| R / Rfree (%) | 16.3 / 18.1 |
Other elements in 6cac:
The structure of Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop also contains other interesting chemical elements:
| Nickel | (Ni) | 5 atoms |
| Cobalt | (Co) | 4 atoms |
| Zinc | (Zn) | 4 atoms |
| Calcium | (Ca) | 4 atoms |
Cadmium Binding Sites:
The binding sites of Cadmium atom in the Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop
(pdb code 6cac). This binding sites where shown within
5.0 Angstroms radius around Cadmium atom.
In total 4 binding sites of Cadmium where determined in the Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop, PDB code: 6cac:
Jump to Cadmium binding site number: 1; 2; 3; 4;
In total 4 binding sites of Cadmium where determined in the Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop, PDB code: 6cac:
Jump to Cadmium binding site number: 1; 2; 3; 4;
Cadmium binding site 1 out of 4 in 6cac
Go back to
Cadmium Binding Sites List in 6cac
Cadmium binding site 1 out
of 4 in the Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Cadmium with other atoms in the Cd binding
site number 1 of Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop within 5.0Å range:
|
Cadmium binding site 2 out of 4 in 6cac
Go back to
Cadmium Binding Sites List in 6cac
Cadmium binding site 2 out
of 4 in the Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Cadmium with other atoms in the Cd binding
site number 2 of Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop within 5.0Å range:
|
Cadmium binding site 3 out of 4 in 6cac
Go back to
Cadmium Binding Sites List in 6cac
Cadmium binding site 3 out
of 4 in the Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Cadmium with other atoms in the Cd binding
site number 3 of Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop within 5.0Å range:
|
Cadmium binding site 4 out of 4 in 6cac
Go back to
Cadmium Binding Sites List in 6cac
Cadmium binding site 4 out
of 4 in the Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Cadmium with other atoms in the Cd binding
site number 4 of Crystal Structure of Ndm-1 Metallo-Beta-Lactamase Harboring An Insertion of A Pro Residue in L3 Loop within 5.0Å range:
|
Reference:
A.R.Palacios,
M.F.Mojica,
E.Giannini,
M.A.Taracila,
C.R.Bethel,
P.M.Alzari,
L.H.Otero,
S.Klinke,
L.I.Llarrull,
R.A.Bonomo,
A.J.Vila.
The Reaction Mechanism of Metallo-Beta-Lactamases Is Tuned By the Conformation of An Active-Site Mobile Loop. Antimicrob. Agents V. 63 2019CHEMOTHER..
ISSN: ESSN 1098-6596
PubMed: 30348667
DOI: 10.1128/AAC.01754-18
Page generated: Sat Dec 12 08:28:09 2020
ISSN: ESSN 1098-6596
PubMed: 30348667
DOI: 10.1128/AAC.01754-18
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