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Magnesium in PDB 1pvg: Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II

Enzymatic activity of Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II

All present enzymatic activity of Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II:
5.99.1.3;

Protein crystallography data

The structure of Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II, PDB code: 1pvg was solved by S.Classen, S.Olland, J.M.Berger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.75 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 58.456, 71.081, 216.132, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 24.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II (pdb code 1pvg). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II, PDB code: 1pvg:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1pvg

Go back to Magnesium Binding Sites List in 1pvg
Magnesium binding site 1 out of 2 in the Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg903

b:22.2
occ:1.00
O2G A:ANP901 2.0 20.1 1.0
O A:HOH904 2.1 18.9 1.0
O1B A:ANP901 2.1 20.5 1.0
O1A A:ANP901 2.1 20.4 1.0
OD1 A:ASN70 2.2 12.9 1.0
O A:HOH936 2.2 23.5 1.0
PB A:ANP901 3.1 21.9 1.0
CG A:ASN70 3.1 13.0 1.0
PA A:ANP901 3.3 21.5 1.0
PG A:ANP901 3.3 22.4 1.0
O3A A:ANP901 3.4 22.7 1.0
ND2 A:ASN70 3.5 13.0 1.0
N3B A:ANP901 3.6 22.2 1.0
O A:HOH928 3.9 24.2 1.0
O5' A:ANP901 4.0 21.4 1.0
OE1 A:GLU66 4.1 19.6 1.0
O A:HOH999 4.1 32.5 1.0
O1G A:ANP901 4.2 21.3 1.0
O3G A:ANP901 4.3 23.4 1.0
CA A:GLY140 4.3 15.3 1.0
CA A:GLY145 4.3 14.1 1.0
O A:GLU66 4.3 13.5 1.0
O2A A:ANP901 4.4 20.4 1.0
O2B A:ANP901 4.4 21.6 1.0
CB A:ASN70 4.5 13.0 1.0
N A:GLY145 4.6 14.6 1.0
OD2 A:ASP73 4.6 18.6 1.0
N A:ALA146 4.8 13.4 1.0
CA A:ASN70 4.8 13.4 1.0
N A:ASN70 4.8 13.6 1.0
C A:GLY145 4.9 14.0 1.0
NZ A:LYS367 5.0 25.1 1.0

Magnesium binding site 2 out of 2 in 1pvg

Go back to Magnesium Binding Sites List in 1pvg
Magnesium binding site 2 out of 2 in the Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Atpase Region of Saccharomyces Cerevisiae Topoisomerase II within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg904

b:23.9
occ:1.00
O2G B:ANP902 2.0 23.1 1.0
O1B B:ANP902 2.0 25.1 1.0
O1A B:ANP902 2.1 24.0 1.0
O B:HOH911 2.1 22.5 1.0
OD1 B:ASN70 2.2 12.4 1.0
O B:HOH912 2.2 22.7 1.0
PB B:ANP902 3.1 24.9 1.0
CG B:ASN70 3.1 13.6 1.0
PA B:ANP902 3.2 24.2 1.0
PG B:ANP902 3.3 23.4 1.0
O3A B:ANP902 3.4 24.1 1.0
ND2 B:ASN70 3.5 13.0 1.0
N3B B:ANP902 3.6 23.6 1.0
O B:HOH932 3.9 27.2 1.0
O5' B:ANP902 4.0 25.7 1.0
OE1 B:GLU66 4.1 17.8 1.0
O B:HOH1042 4.1 36.6 1.0
O1G B:ANP902 4.2 22.7 1.0
O3G B:ANP902 4.3 24.8 1.0
CA B:GLY140 4.3 16.4 1.0
CA B:GLY145 4.4 14.0 1.0
O2B B:ANP902 4.4 23.8 1.0
O B:GLU66 4.4 14.5 1.0
O2A B:ANP902 4.4 21.6 1.0
CB B:ASN70 4.5 14.5 1.0
N B:GLY145 4.6 14.8 1.0
OD2 B:ASP73 4.7 20.2 1.0
N B:ALA146 4.7 13.7 1.0
CA B:ASN70 4.8 14.4 1.0
N B:ASN70 4.9 14.5 1.0
NZ B:LYS367 4.9 24.8 1.0
C B:GLY145 5.0 14.6 1.0

Reference:

S.Classen, S.Olland, J.M.Berger. Structure of the Topoisomerase II Atpase Region and Its Mechanism of Inhibition By the Chemotherapeutic Agent Icrf-187 Proc.Natl.Acad.Sci.Usa V. 100 10629 2003.
ISSN: ISSN 0027-8424
PubMed: 12963818
DOI: 10.1073/PNAS.1832879100
Page generated: Tue Aug 13 10:56:49 2024

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