Atomistry » Platinum » PDB 4nsj-5bna » 4qot
Atomistry »
  Platinum »
    PDB 4nsj-5bna »
      4qot »

Platinum in PDB 4qot: Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion

Enzymatic activity of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion

All present enzymatic activity of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion:
3.6.3.54;

Protein crystallography data

The structure of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion, PDB code: 4qot was solved by B.D.Belviso, A.Galliani, R.Caliandro, F.Arnesano, G.Natile, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.49 / 2.20
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 78.055, 78.055, 54.628, 90.00, 90.00, 120.00
R / Rfree (%) 18.8 / 23.9

Platinum Binding Sites:

The binding sites of Platinum atom in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion (pdb code 4qot). This binding sites where shown within 5.0 Angstroms radius around Platinum atom.
In total 2 binding sites of Platinum where determined in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion, PDB code: 4qot:
Jump to Platinum binding site number: 1; 2;

Platinum binding site 1 out of 2 in 4qot

Go back to Platinum Binding Sites List in 4qot
Platinum binding site 1 out of 2 in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 1 of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Pt101

b:26.8
occ:0.40
SG B:CYS15 2.3 25.7 1.0
SG B:CYS12 2.3 24.0 1.0
SG A:CYS15 2.3 28.6 1.0
SG A:CYS12 2.3 22.8 1.0
CB A:CYS12 3.4 20.4 1.0
CB B:CYS12 3.5 19.2 1.0
CB A:CYS15 3.5 20.7 1.0
CB B:CYS15 3.6 19.9 1.0
N A:CYS15 3.6 21.0 1.0
N B:CYS12 3.7 31.1 1.0
N B:CYS15 3.7 19.5 1.0
N A:CYS12 4.0 29.5 1.0
CA A:CYS15 4.0 21.0 1.0
OG1 B:THR11 4.0 34.2 1.0
CA B:CYS15 4.0 22.0 1.0
CA B:CYS12 4.1 19.1 1.0
CA A:CYS12 4.1 21.4 1.0
OG1 A:THR11 4.4 21.7 1.0
C A:THR11 4.5 22.8 1.0
O A:CYS12 4.5 24.6 1.0
O B:CYS12 4.5 19.0 1.0
C B:CYS12 4.5 18.8 1.0
C A:CYS12 4.5 30.5 1.0
C A:GLY14 4.6 23.2 1.0
C B:GLY14 4.6 24.9 1.0
C B:THR11 4.7 22.7 1.0
N B:THR11 4.7 17.7 1.0
N A:THR11 4.9 25.1 1.0
O A:THR11 4.9 29.2 1.0
CA B:THR11 4.9 22.6 1.0
CA A:GLY14 5.0 22.0 1.0
CB B:THR11 5.0 22.3 1.0

Platinum binding site 2 out of 2 in 4qot

Go back to Platinum Binding Sites List in 4qot
Platinum binding site 2 out of 2 in the Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion


Mono view


Stereo pair view

A full contact list of Platinum with other atoms in the Pt binding site number 2 of Crystal Structure of Human Copper Chaperone Bound to the Platinum Ion within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Pt101

b:49.6
occ:0.25
O1 B:SO4104 1.9 46.1 0.4
OE1 B:GLU5 2.1 52.0 0.4
NZ B:LYS3 2.1 39.4 0.3
OE2 B:GLU5 2.3 31.3 0.4
SG B:CYS41 2.4 30.2 0.4
CD B:GLU5 2.4 49.4 0.4
SG B:CYS41 2.8 61.5 0.6
CE B:LYS3 2.8 35.0 0.3
CB B:CYS41 3.2 4.6 0.6
S B:SO4104 3.2 47.5 0.4
CB B:CYS41 3.2 30.0 0.4
O2 B:SO4104 3.6 46.0 0.4
O3 B:SO4104 3.7 48.8 0.4
CG B:GLU5 3.8 51.7 0.4
CD B:LYS3 3.9 34.2 0.3
OE1 B:GLU5 4.1 35.0 0.6
CD B:GLU5 4.2 27.4 0.6
O4 B:SO4104 4.3 44.4 0.4
CA B:CYS41 4.4 39.4 0.4
OE2 B:GLU5 4.4 21.3 0.6
CA B:CYS41 4.5 10.1 0.6
CG B:GLU5 4.6 22.8 0.6
CB B:GLU5 4.7 19.2 0.6
CB B:GLU5 4.7 49.1 0.4
CG B:LYS3 4.8 32.7 0.3

Reference:

B.D.Belviso, A.Galliani, A.Lasorsa, V.Mirabelli, R.Caliandro, F.Arnesano, G.Natile. Oxaliplatin Binding to Human Copper Chaperone ATOX1 and Protein Dimerization Inorg.Chem. V. 55 6563 2016.
ISSN: ISSN 0020-1669
PubMed: 27305454
DOI: 10.1021/ACS.INORGCHEM.6B00750
Page generated: Wed Dec 16 02:05:00 2020

Last articles

Zn in 7NN0
Zn in 7NIO
Zn in 7LUP
Zn in 7M1Y
Zn in 7LO4
Zn in 7KWO
Zn in 7KJY
Zn in 7KCQ
Zn in 7KC2
Zn in 7KCB
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy