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Platinum in PDB 5f9u: X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees

Enzymatic activity of X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees

All present enzymatic activity of X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees:
3.2.1.17;

Protein crystallography data

The structure of X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees, PDB code: 5f9u was solved by I.Russo Krauss, G.Ferraro, A.Pica, A.Merlino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.71 / 1.85
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 78.785, 78.785, 36.975, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 23.3

Other elements in 5f9u:

The structure of X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Platinum Binding Sites:

The binding sites of Platinum atom in the X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees (pdb code 5f9u). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total 2 binding sites of Platinum where determined in the X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees, PDB code: 5f9u:
Jump to Platinum binding site number: 1; 2;

Platinum binding site 1 out of 2 in 5f9u

Go back to Platinum Binding Sites List in 5f9u
Platinum binding site 1 out of 2 in the X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt202

b:50.6
occ:0.50
PT1 A:CPT202 0.0 50.6 0.5
N1 A:CPT202 2.0 45.4 0.5
ND1 A:HIS15 2.1 48.7 1.0
N2 A:CPT202 2.2 46.1 0.5
CL2 A:CPT202 2.2 40.1 0.5
CE1 A:HIS15 3.1 48.1 1.0
CG A:HIS15 3.1 38.9 1.0
CB A:HIS15 3.4 33.3 1.0
CA A:HIS15 3.5 31.3 1.0
O A:HIS15 4.1 29.7 1.0
C A:HIS15 4.2 26.8 1.0
NE2 A:HIS15 4.2 46.0 1.0
CD2 A:HIS15 4.2 40.3 1.0
O A:ARG14 4.5 28.1 1.0
O A:HOH321 4.6 48.0 1.0
N A:HIS15 4.6 30.0 1.0
OG1 A:THR89 4.9 26.6 1.0
C A:ARG14 4.9 30.9 1.0
O A:HOH345 4.9 46.7 1.0
CG2 A:THR89 5.0 29.5 1.0

Platinum binding site 2 out of 2 in 5f9u

Go back to Platinum Binding Sites List in 5f9u
Platinum binding site 2 out of 2 in the X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 2 of X-Ray Structure of the Adduct Between Hen Egg White Lysozyme and Cisplatin Upon 24 Hours of Incubation at 20 Degrees within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt203

b:58.0
occ:0.50
PT1 A:CPT203 0.0 58.0 0.5
N1 A:CPT203 2.1 59.1 0.5
NH1 A:ARG14 2.1 57.6 1.0
O A:HOH311 2.2 30.3 0.5
CL2 A:CPT203 2.2 48.0 0.5
NE2 A:HIS15 2.3 46.0 1.0
CZ A:ARG14 3.2 61.9 1.0
CE1 A:HIS15 3.2 48.1 1.0
CD2 A:HIS15 3.3 40.3 1.0
NE A:ARG14 3.4 55.7 1.0
O A:HOH378 3.6 24.6 0.5
OD1 A:ASP87 4.3 30.2 1.0
O A:HOH336 4.3 53.0 1.0
ND1 A:HIS15 4.3 48.7 1.0
NH2 A:ARG14 4.3 60.7 1.0
CG A:HIS15 4.4 38.9 1.0
OG1 A:THR89 4.7 26.6 1.0
CD A:ARG14 4.9 50.6 1.0
CG1 A:ILE88 4.9 27.8 1.0

Reference:

G.Ferraro, A.Pica, I.Russo Krauss, F.Pane, A.Amoresano, A.Merlino. Effect of Temperature on the Interaction of Cisplatin with the Model Protein Hen Egg White Lysozyme. J.Biol.Inorg.Chem. V. 21 433 2016.
ISSN: ESSN 1432-1327
PubMed: 27040953
DOI: 10.1007/S00775-016-1352-0
Page generated: Thu Oct 10 11:34:24 2024

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