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Aluminium in PDB 1z5b: Topoisomerase VI-B, Adp ALF4- Bound Dimer Form

Enzymatic activity of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form

All present enzymatic activity of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form:
5.99.1.3;

Protein crystallography data

The structure of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form, PDB code: 1z5b was solved by K.D.Corbett, J.M.Berger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.00
Space group P 32 1 2
Cell size a, b, c (Å), α, β, γ (°) 74.077, 74.077, 344.381, 90.00, 90.00, 120.00
R / Rfree (%) 17.9 / 20.8

Other elements in 1z5b:

The structure of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form also contains other interesting chemical elements:

Fluorine (F) 8 atoms
Magnesium (Mg) 3 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form (pdb code 1z5b). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total 2 binding sites of Aluminium where determined in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form, PDB code: 1z5b:
Jump to Aluminium binding site number: 1; 2;

Aluminium binding site 1 out of 2 in 1z5b

Go back to Aluminium Binding Sites List in 1z5b
Aluminium binding site 1 out of 2 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Al3001

b:19.4
occ:1.00
AL A:ALF3001 0.0 19.4 1.0
F3 A:ALF3001 1.8 20.7 1.0
F2 A:ALF3001 1.8 19.4 1.0
F4 A:ALF3001 1.8 18.7 1.0
F1 A:ALF3001 1.8 20.6 1.0
O3B A:ADP1001 2.0 15.9 1.0
O A:HOH4002 2.0 14.1 1.0
PB A:ADP1001 3.1 18.1 1.0
MG A:MG2001 3.2 20.1 1.0
O1B A:ADP1001 3.5 16.2 1.0
O3A A:ADP1001 3.6 17.7 1.0
NZ A:LYS427 3.7 17.6 1.0
O A:HOH4136 3.7 28.3 1.0
N A:GLY111 3.7 7.7 1.0
N A:MET107 4.0 7.4 1.0
N A:TYR108 4.0 7.0 1.0
OE2 A:GLU38 4.0 9.5 1.0
O A:HOH4137 4.1 26.4 1.0
O A:HOH4038 4.1 20.8 1.0
O A:HOH4006 4.1 16.9 1.0
CA A:GLY106 4.1 7.7 1.0
N A:GLY109 4.1 6.7 1.0
CA A:GLY111 4.2 7.2 1.0
O1A A:ADP1001 4.2 18.6 1.0
N A:LEU110 4.3 7.0 1.0
PA A:ADP1001 4.4 18.6 1.0
CB A:TYR108 4.5 7.3 1.0
O2B A:ADP1001 4.5 15.2 1.0
C A:GLY106 4.6 7.7 1.0
CA A:TYR108 4.6 7.2 1.0
CD2 A:TYR108 4.8 7.4 1.0
C A:LEU110 4.8 8.0 1.0
C A:TYR108 4.8 6.9 1.0
CA A:GLY109 4.9 6.9 1.0
C A:MET107 5.0 7.2 1.0
CA A:LEU110 5.0 7.5 1.0

Aluminium binding site 2 out of 2 in 1z5b

Go back to Aluminium Binding Sites List in 1z5b
Aluminium binding site 2 out of 2 in the Topoisomerase VI-B, Adp ALF4- Bound Dimer Form


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Topoisomerase VI-B, Adp ALF4- Bound Dimer Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al3002

b:21.2
occ:1.00
AL B:ALF3002 0.0 21.2 1.0
F4 B:ALF3002 1.8 20.9 1.0
F2 B:ALF3002 1.8 24.1 1.0
F3 B:ALF3002 1.8 21.2 1.0
F1 B:ALF3002 1.8 19.2 1.0
O3B B:ADP1002 1.9 18.6 1.0
O B:HOH3003 2.1 15.8 1.0
PB B:ADP1002 3.1 17.4 1.0
MG B:MG2002 3.3 18.4 1.0
O1B B:ADP1002 3.5 16.4 1.0
O3A B:ADP1002 3.7 15.6 1.0
NZ B:LYS427 3.7 23.3 1.0
O B:HOH3165 3.8 31.3 1.0
N B:GLY111 3.9 7.1 1.0
N B:TYR108 3.9 6.7 1.0
N B:MET107 3.9 7.3 1.0
CE B:LYS427 4.0 19.6 1.0
CA B:GLY106 4.1 7.7 1.0
O B:HOH3089 4.1 27.3 1.0
OE2 B:GLU38 4.1 9.9 1.0
N B:GLY109 4.2 7.1 1.0
O B:HOH3025 4.2 16.4 1.0
CA B:GLY111 4.3 7.4 1.0
O1A B:ADP1002 4.3 17.9 1.0
O B:HOH3008 4.3 15.3 1.0
N B:LEU110 4.3 7.1 1.0
O2B B:ADP1002 4.4 16.7 1.0
CB B:TYR108 4.4 6.7 1.0
C B:GLY106 4.5 7.5 1.0
PA B:ADP1002 4.6 17.4 1.0
CA B:TYR108 4.6 7.0 1.0
CD2 B:TYR108 4.7 8.5 1.0
C B:TYR108 4.8 7.0 1.0
C B:MET107 4.9 6.8 1.0
CA B:GLY109 4.9 7.0 1.0
CA B:MET107 4.9 6.9 1.0
CG B:TYR108 5.0 8.1 1.0
C B:LEU110 5.0 6.8 1.0

Reference:

K.D.Corbett, J.M.Berger. Structural Dissection of Atp Turnover in the Prototypical Ghl Atpase Topovi. Structure V. 13 873 2005.
ISSN: ISSN 0969-2126
PubMed: 15939019
DOI: 10.1016/J.STR.2005.03.013
Page generated: Sat Dec 12 01:30:47 2020

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