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Fluorine in PDB 2wz6: G93A SOD1 Mutant Complexed with Quinazoline.

Enzymatic activity of G93A SOD1 Mutant Complexed with Quinazoline.

All present enzymatic activity of G93A SOD1 Mutant Complexed with Quinazoline.:
1.15.1.1;

Protein crystallography data

The structure of G93A SOD1 Mutant Complexed with Quinazoline., PDB code: 2wz6 was solved by S.V.Antonyuk, R.W.Strange, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.85 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 38.996, 68.025, 50.633, 90.00, 105.88, 90.00
R / Rfree (%) 19.5 / 24.8

Other elements in 2wz6:

The structure of G93A SOD1 Mutant Complexed with Quinazoline. also contains other interesting chemical elements:

Copper (Cu) 2 atoms
Zinc (Zn) 4 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the G93A SOD1 Mutant Complexed with Quinazoline. (pdb code 2wz6). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the G93A SOD1 Mutant Complexed with Quinazoline., PDB code: 2wz6:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in 2wz6

Go back to Fluorine Binding Sites List in 2wz6
Fluorine binding site 1 out of 6 in the G93A SOD1 Mutant Complexed with Quinazoline.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of G93A SOD1 Mutant Complexed with Quinazoline. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F204

b:36.5
occ:1.00
 F13 A:ZO0204 0.0 36.5 1.0
C11 A:ZO0204 1.3 35.0 1.0
F14 A:ZO0204 2.1 32.9 1.0
F12 A:ZO0204 2.2 38.1 1.0
C2 A:ZO0204 2.2 33.1 1.0
N3 A:ZO0204 2.8 33.0 1.0
O A:ILE99 3.0 17.1 1.0
N1 A:ZO0204 3.1 29.4 1.0
N A:VAL31 3.3 12.5 1.0
O A:VAL31 3.3 13.2 1.0
CB A:LYS30 3.4 14.0 1.0
CA A:LYS30 3.7 12.7 1.0
C A:ILE99 3.8 15.6 1.0
C A:LYS30 3.8 12.8 1.0
N A:ILE99 3.9 18.6 1.0
C A:VAL31 3.9 14.0 1.0
C4 A:ZO0204 4.1 31.8 1.0
CG A:LYS30 4.1 15.8 1.0
CE A:LYS30 4.2 16.1 0.5
C6 A:ZO0204 4.3 31.0 1.0
CA A:VAL31 4.3 12.5 1.0
OG A:SER98 4.4 19.6 1.0
CE3 A:TRP32 4.4 14.9 1.0
CB A:TRP32 4.5 12.8 1.0
N A:GLU100 4.5 14.0 1.0
CA A:ILE99 4.5 16.8 1.0
C A:SER98 4.6 19.4 1.0
N A:TRP32 4.6 13.1 1.0
CA A:SER98 4.7 18.4 1.0
NZ A:LYS30 4.7 18.9 0.5
C5 A:ZO0204 4.7 31.2 1.0
CD A:LYS30 4.7 17.1 0.5
O A:HOH461 4.8 35.2 1.0
O A:LYS30 4.8 12.5 1.0
CA A:GLU100 4.8 14.6 1.0
CB A:GLU100 4.9 16.1 1.0

Fluorine binding site 2 out of 6 in 2wz6

Go back to Fluorine Binding Sites List in 2wz6
Fluorine binding site 2 out of 6 in the G93A SOD1 Mutant Complexed with Quinazoline.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of G93A SOD1 Mutant Complexed with Quinazoline. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F204

b:32.9
occ:1.00
 F14 A:ZO0204 0.0 32.9 1.0
C11 A:ZO0204 1.3 35.0 1.0
F12 A:ZO0204 2.1 38.1 1.0
F13 A:ZO0204 2.1 36.5 1.0
C2 A:ZO0204 2.4 33.1 1.0
N1 A:ZO0204 2.7 29.4 1.0
OG A:SER98 2.9 19.6 1.0
N3 A:ZO0204 3.6 33.0 1.0
N A:ILE99 3.7 18.6 1.0
O A:HOH461 3.8 35.2 1.0
C A:SER98 3.8 19.4 1.0
O A:ILE99 3.9 17.1 1.0
C A:ILE99 4.0 15.6 1.0
CB A:SER98 4.0 19.5 1.0
CA A:SER98 4.1 18.4 1.0
C6 A:ZO0204 4.1 31.0 1.0
O A:SER98 4.4 19.1 1.0
CA A:ILE99 4.4 16.8 1.0
O A:VAL31 4.5 13.2 1.0
N A:GLU100 4.5 14.0 1.0
O A:HOH329 4.7 34.4 1.0
C4 A:ZO0204 4.8 31.8 1.0
C7 A:ZO0204 4.9 28.9 1.0
CB A:GLU100 4.9 16.1 1.0
OE1 A:GLU100 4.9 23.9 0.7
NZ A:LYS30 5.0 18.9 0.5
CE A:LYS30 5.0 16.1 0.5

Fluorine binding site 3 out of 6 in 2wz6

Go back to Fluorine Binding Sites List in 2wz6
Fluorine binding site 3 out of 6 in the G93A SOD1 Mutant Complexed with Quinazoline.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of G93A SOD1 Mutant Complexed with Quinazoline. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F204

b:38.1
occ:1.00
 F12 A:ZO0204 0.0 38.1 1.0
C11 A:ZO0204 1.3 35.0 1.0
F14 A:ZO0204 2.1 32.9 1.0
F13 A:ZO0204 2.2 36.5 1.0
C2 A:ZO0204 2.3 33.1 1.0
O A:HOH461 2.7 35.2 1.0
N3 A:ZO0204 2.8 33.0 1.0
CE A:LYS30 2.9 16.1 0.5
NZ A:LYS30 2.9 18.9 0.5
N1 A:ZO0204 3.4 29.4 1.0
OE1 A:GLU100 3.9 23.9 0.7
CG A:LYS30 3.9 15.8 1.0
CB A:LYS30 3.9 14.0 1.0
O A:HOH334 3.9 46.6 1.0
CD A:LYS30 4.0 17.1 0.5
C4 A:ZO0204 4.1 31.8 1.0
O A:ILE99 4.5 17.1 1.0
C6 A:ZO0204 4.6 31.0 1.0
CA A:LYS30 4.7 12.7 1.0
C16 A:ZO0204 4.7 33.7 1.0
CD A:GLU100 4.7 22.8 1.0
CB A:GLU100 4.8 16.1 1.0
OG A:SER98 4.8 19.6 1.0
C5 A:ZO0204 4.9 31.2 1.0
N15 A:ZO0204 5.0 33.5 1.0

Fluorine binding site 4 out of 6 in 2wz6

Go back to Fluorine Binding Sites List in 2wz6
Fluorine binding site 4 out of 6 in the G93A SOD1 Mutant Complexed with Quinazoline.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of G93A SOD1 Mutant Complexed with Quinazoline. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:F206

b:33.9
occ:1.00
 F13 F:ZO0206 0.0 33.9 1.0
C11 F:ZO0206 1.3 34.9 1.0
F14 F:ZO0206 2.1 32.8 1.0
F12 F:ZO0206 2.2 38.0 1.0
C2 F:ZO0206 2.2 36.0 1.0
N3 F:ZO0206 2.8 37.6 1.0
O F:ILE99 2.9 17.2 1.0
N1 F:ZO0206 3.1 35.2 1.0
N F:VAL31 3.3 12.4 1.0
O F:VAL31 3.3 13.5 1.0
CB F:LYS30 3.3 14.2 1.0
CA F:LYS30 3.6 12.9 1.0
C F:LYS30 3.8 12.6 1.0
C F:ILE99 3.8 15.5 1.0
C F:VAL31 3.9 13.3 1.0
N F:ILE99 3.9 17.9 1.0
CG F:LYS30 4.0 17.0 1.0
CD F:LYS30 4.1 22.2 1.0
C4 F:ZO0206 4.1 37.2 1.0
CA F:VAL31 4.3 12.0 1.0
C6 F:ZO0206 4.3 35.3 1.0
OG F:SER98 4.3 23.0 1.0
CB F:TRP32 4.4 12.5 1.0
CE3 F:TRP32 4.5 14.6 1.0
CA F:ILE99 4.5 16.4 1.0
N F:GLU100 4.5 14.2 1.0
N F:TRP32 4.6 12.9 1.0
C F:SER98 4.6 18.9 1.0
CA F:SER98 4.7 18.6 1.0
C5 F:ZO0206 4.7 36.5 1.0
O F:LYS30 4.8 11.8 1.0
CE F:LYS30 4.8 21.9 0.5
O F:HOH484 4.9 32.3 1.0
CA F:GLU100 4.9 14.1 1.0
CA F:TRP32 5.0 12.1 1.0

Fluorine binding site 5 out of 6 in 2wz6

Go back to Fluorine Binding Sites List in 2wz6
Fluorine binding site 5 out of 6 in the G93A SOD1 Mutant Complexed with Quinazoline.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of G93A SOD1 Mutant Complexed with Quinazoline. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:F206

b:32.8
occ:1.00
 F14 F:ZO0206 0.0 32.8 1.0
C11 F:ZO0206 1.3 34.9 1.0
F12 F:ZO0206 2.1 38.0 1.0
F13 F:ZO0206 2.1 33.9 1.0
C2 F:ZO0206 2.4 36.0 1.0
OG F:SER98 2.8 23.0 1.0
N1 F:ZO0206 2.8 35.2 1.0
O F:HOH484 3.1 32.3 1.0
N F:ILE99 3.6 17.9 1.0
N3 F:ZO0206 3.6 37.6 1.0
O F:ILE99 3.7 17.2 1.0
C F:SER98 3.8 18.9 1.0
C F:ILE99 3.9 15.5 1.0
CB F:SER98 4.0 19.1 1.0
CA F:SER98 4.0 18.6 1.0
O F:HOH497 4.1 31.0 1.0
C6 F:ZO0206 4.2 35.3 1.0
CA F:ILE99 4.3 16.4 1.0
N F:GLU100 4.4 14.2 1.0
O F:VAL31 4.4 13.5 1.0
O F:SER98 4.5 19.4 1.0
C4 F:ZO0206 4.8 37.2 1.0

Fluorine binding site 6 out of 6 in 2wz6

Go back to Fluorine Binding Sites List in 2wz6
Fluorine binding site 6 out of 6 in the G93A SOD1 Mutant Complexed with Quinazoline.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of G93A SOD1 Mutant Complexed with Quinazoline. within 5.0Å range:
probe atom residue distance (Å) B Occ
F:F206

b:38.0
occ:1.00
 F12 F:ZO0206 0.0 38.0 1.0
C11 F:ZO0206 1.3 34.9 1.0
F14 F:ZO0206 2.1 32.8 1.0
F13 F:ZO0206 2.2 33.9 1.0
C2 F:ZO0206 2.3 36.0 1.0
N3 F:ZO0206 2.7 37.6 1.0
O F:HOH497 3.0 31.0 1.0
CD F:LYS30 3.1 22.2 1.0
CE F:LYS30 3.3 21.9 0.5
O F:HOH484 3.4 32.3 1.0
N1 F:ZO0206 3.5 35.2 1.0
CG F:LYS30 3.6 17.0 1.0
CB F:LYS30 3.9 14.2 1.0
C4 F:ZO0206 4.0 37.2 1.0
OE1 F:GLU100 4.4 27.2 0.7
O F:ILE99 4.4 17.2 1.0
C6 F:ZO0206 4.6 35.3 1.0
CA F:LYS30 4.6 12.9 1.0
C16 F:ZO0206 4.6 41.9 1.0
O F:HOH488 4.7 40.1 1.0
NZ F:LYS30 4.7 21.4 0.5
OG F:SER98 4.7 23.0 1.0
N15 F:ZO0206 4.8 41.2 1.0
C5 F:ZO0206 4.9 36.5 1.0
CB F:GLU100 4.9 16.4 1.0
C F:ILE99 5.0 15.5 1.0

Reference:

S.Antonyuk, R.W.Strange, S.S.Hasnain. Structural Discovery of Small Molecule Binding Sites in Cu-Zn Human Superoxide Dismutase Familial Amyotrophic Lateral Sclerosis Mutants Provides Insights For Lead Optimization. J.Med.Chem. V. 53 1402 2010.
ISSN: ISSN 0022-2623
PubMed: 20067275
DOI: 10.1021/JM9017948
Page generated: Wed Jul 31 16:31:09 2024

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