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Manganese in PDB 4f6e: Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae

Enzymatic activity of Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae

All present enzymatic activity of Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae:
1.15.1.1;

Protein crystallography data

The structure of Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae, PDB code: 4f6e was solved by Y.Sheng, D.Cascio, J.S.Valentine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.65 / 1.60
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 65.540, 66.250, 66.620, 112.58, 103.63, 110.27
R / Rfree (%) 16.4 / 19.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae (pdb code 4f6e). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae, PDB code: 4f6e:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in 4f6e

Go back to Manganese Binding Sites List in 4f6e
Manganese binding site 1 out of 4 in the Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn301

b:9.9
occ:1.00
OD2 A:ASP168 2.1 8.8 1.0
NE2 A:HIS81 2.2 9.6 1.0
NE2 A:HIS172 2.2 8.0 1.0
NE2 A:HIS26 2.3 10.2 1.0
O A:HOH403 2.4 11.0 1.0
CG A:ASP168 3.1 11.9 1.0
CE1 A:HIS81 3.1 8.2 1.0
CD2 A:HIS172 3.1 9.5 1.0
CD2 A:HIS81 3.2 8.2 1.0
CE1 A:HIS26 3.2 8.8 1.0
CE1 A:HIS172 3.2 10.2 1.0
CD2 A:HIS26 3.3 9.2 1.0
OD1 A:ASP168 3.5 9.2 1.0
ND1 A:HIS81 4.3 9.5 1.0
CG A:HIS172 4.3 7.7 1.0
ND1 A:HIS172 4.3 9.8 1.0
CG A:HIS81 4.3 9.8 1.0
ND1 A:HIS26 4.3 8.1 1.0
CZ2 A:TRP133 4.4 9.6 1.0
CB A:ASP168 4.4 8.2 1.0
CG A:HIS26 4.4 8.1 1.0
CB A:TRP170 4.5 7.8 1.0
CH2 A:TRP133 4.7 9.1 1.0
CG A:TRP170 4.8 8.4 1.0
NE2 A:GLN154 4.8 11.2 1.0
CB A:ALA173 4.9 7.2 1.0

Manganese binding site 2 out of 4 in 4f6e

Go back to Manganese Binding Sites List in 4f6e
Manganese binding site 2 out of 4 in the Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn301

b:9.3
occ:1.00
OD2 B:ASP168 2.1 10.0 1.0
NE2 B:HIS26 2.2 8.7 1.0
NE2 B:HIS172 2.2 7.8 1.0
O B:HOH401 2.3 9.1 1.0
NE2 B:HIS81 2.3 9.7 1.0
CG B:ASP168 3.2 7.8 1.0
CD2 B:HIS172 3.2 8.6 1.0
CD2 B:HIS26 3.2 9.8 1.0
CE1 B:HIS26 3.2 8.7 1.0
CD2 B:HIS81 3.2 10.0 1.0
CE1 B:HIS172 3.2 8.8 1.0
CE1 B:HIS81 3.2 7.6 1.0
OD1 B:ASP168 3.5 9.5 1.0
ND1 B:HIS26 4.3 8.1 1.0
ND1 B:HIS172 4.3 9.9 1.0
CG B:HIS26 4.3 9.2 1.0
CG B:HIS172 4.3 8.2 1.0
ND1 B:HIS81 4.3 7.2 1.0
CG B:HIS81 4.4 8.9 1.0
CZ2 B:TRP133 4.4 9.6 1.0
CB B:ASP168 4.4 7.8 1.0
CB B:TRP170 4.5 9.4 1.0
CG B:TRP170 4.7 9.6 1.0
CH2 B:TRP133 4.7 8.6 1.0
NE2 B:GLN154 4.8 11.3 1.0
CB B:ALA173 4.9 8.6 1.0

Manganese binding site 3 out of 4 in 4f6e

Go back to Manganese Binding Sites List in 4f6e
Manganese binding site 3 out of 4 in the Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn301

b:8.9
occ:1.00
OD2 C:ASP168 2.1 9.2 1.0
NE2 C:HIS81 2.2 9.0 1.0
NE2 C:HIS172 2.2 7.2 1.0
NE2 C:HIS26 2.3 7.2 1.0
O C:HOH402 2.3 10.7 1.0
CG C:ASP168 3.1 7.2 1.0
CD2 C:HIS172 3.2 8.5 1.0
CD2 C:HIS81 3.2 8.2 1.0
CE1 C:HIS81 3.2 7.1 1.0
CE1 C:HIS26 3.2 10.3 1.0
CE1 C:HIS172 3.2 9.4 1.0
CD2 C:HIS26 3.2 7.9 1.0
OD1 C:ASP168 3.5 8.0 1.0
ND1 C:HIS81 4.3 6.9 1.0
ND1 C:HIS172 4.3 9.3 1.0
CG C:HIS81 4.3 6.3 1.0
CG C:HIS172 4.3 7.5 1.0
ND1 C:HIS26 4.3 8.8 1.0
CZ2 C:TRP133 4.3 10.4 1.0
CB C:ASP168 4.4 7.0 1.0
CG C:HIS26 4.4 7.3 1.0
CB C:TRP170 4.5 9.6 1.0
CH2 C:TRP133 4.7 10.5 1.0
CG C:TRP170 4.7 6.8 1.0
NE2 C:GLN154 4.8 10.0 1.0
CB C:ALA173 4.9 6.8 1.0

Manganese binding site 4 out of 4 in 4f6e

Go back to Manganese Binding Sites List in 4f6e
Manganese binding site 4 out of 4 in the Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn302

b:10.8
occ:1.00
OD2 D:ASP168 2.1 10.2 1.0
NE2 D:HIS81 2.2 11.2 1.0
NE2 D:HIS26 2.3 10.8 1.0
NE2 D:HIS172 2.3 10.3 1.0
O D:HOH403 2.3 12.0 1.0
CG D:ASP168 3.1 10.3 1.0
CD2 D:HIS81 3.2 11.1 1.0
CD2 D:HIS172 3.2 10.7 1.0
CE1 D:HIS26 3.2 12.0 1.0
CD2 D:HIS26 3.2 11.2 1.0
CE1 D:HIS81 3.3 12.7 1.0
CE1 D:HIS172 3.3 12.7 1.0
OD1 D:ASP168 3.5 9.7 1.0
CG D:HIS81 4.3 9.7 1.0
ND1 D:HIS26 4.3 8.8 1.0
ND1 D:HIS81 4.3 12.2 1.0
CG D:HIS172 4.3 9.8 1.0
ND1 D:HIS172 4.4 10.0 1.0
CG D:HIS26 4.4 9.9 1.0
CB D:ASP168 4.4 8.7 1.0
CZ2 D:TRP133 4.4 10.1 1.0
CB D:TRP170 4.6 11.6 1.0
CG D:TRP170 4.7 8.1 1.0
NE2 D:GLN154 4.8 9.2 1.0
CH2 D:TRP133 4.8 9.0 1.0
CB D:ALA173 5.0 11.1 1.0

Reference:

Y.Sheng, D.Cascio, J.S.Valentine. Crystal Structure of the K182R, A183P Mutant Manganese Superoxide Dismutase From Sacchromyces Cerevisiae To Be Published.
Page generated: Tue Dec 15 04:20:30 2020

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