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Manganese in PDB 1zlz: Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase

Enzymatic activity of Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase

All present enzymatic activity of Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase:
1.15.1.1;

Protein crystallography data

The structure of Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase, PDB code: 1zlz was solved by J.R.Salvador, M.M.Whittaker, J.W.Whittaker, G.B.Jameson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.69 / 1.55
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 46.727, 45.676, 95.859, 90.00, 97.92, 90.00
R / Rfree (%) 18.2 / 22.2

Manganese Binding Sites:

The binding sites of Manganese atom in the Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase (pdb code 1zlz). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase, PDB code: 1zlz:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 1zlz

Go back to Manganese Binding Sites List in 1zlz
Manganese binding site 1 out of 2 in the Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn206

b:16.1
occ:1.00
MN A:MH2206 0.0 16.1 1.0
OD2 A:ASP167 2.0 17.9 1.0
NE2 A:HIS81 2.1 18.1 1.0
NE2 A:HIS171 2.2 16.3 1.0
NE2 A:HIS26 2.2 12.3 1.0
O1 A:MH2206 2.3 15.0 1.0
CG A:ASP167 3.1 13.9 1.0
CE1 A:HIS26 3.1 9.4 1.0
CD2 A:HIS81 3.1 20.5 1.0
CE1 A:HIS81 3.1 16.1 1.0
CE1 A:HIS171 3.1 15.1 1.0
CD2 A:HIS171 3.1 14.6 1.0
CD2 A:HIS26 3.2 18.9 1.0
OD1 A:ASP167 3.4 15.5 1.0
ND1 A:HIS81 4.2 14.8 1.0
CG A:HIS81 4.2 16.3 1.0
ND1 A:HIS26 4.3 15.1 1.0
ND1 A:HIS171 4.3 15.9 1.0
CG A:HIS171 4.3 16.2 1.0
CG A:HIS26 4.3 12.4 1.0
CB A:ASP167 4.3 13.3 1.0
CZ2 A:TRP128 4.6 15.2 1.0
CB A:TRP169 4.6 17.7 1.0
NE2 A:GLN146 4.7 14.4 1.0
CG A:TRP169 4.9 17.3 1.0
CB A:ALA172 4.9 15.3 1.0

Manganese binding site 2 out of 2 in 1zlz

Go back to Manganese Binding Sites List in 1zlz
Manganese binding site 2 out of 2 in the Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Re-Evaluation of the Low-Temperature Azide in Mn-Dependent Superoxide Dismutase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn206

b:17.1
occ:1.00
MN B:MH2206 0.0 17.1 1.0
N3 B:AZI1207 1.9 28.0 1.0
OD2 B:ASP167 2.0 16.8 1.0
NE2 B:HIS81 2.1 16.6 1.0
O1 B:MH2206 2.1 15.8 1.0
NE2 B:HIS171 2.2 20.5 1.0
NE2 B:HIS26 2.2 16.4 1.0
N2 B:AZI1207 2.9 29.0 1.0
CE1 B:HIS26 3.0 18.4 1.0
CD2 B:HIS81 3.1 18.4 1.0
CE1 B:HIS171 3.1 20.8 1.0
CG B:ASP167 3.1 13.0 1.0
CE1 B:HIS81 3.1 19.9 1.0
CD2 B:HIS171 3.2 16.1 1.0
CD2 B:HIS26 3.3 15.4 1.0
OD1 B:ASP167 3.5 18.7 1.0
N1 B:AZI1207 4.0 22.8 1.0
ND1 B:HIS26 4.2 16.7 1.0
ND1 B:HIS81 4.2 18.3 1.0
CG B:HIS81 4.2 15.9 1.0
ND1 B:HIS171 4.2 15.3 1.0
CG B:HIS171 4.3 16.6 1.0
CG B:HIS26 4.3 14.3 1.0
CB B:ASP167 4.4 17.6 1.0
NE2 B:GLN146 4.7 17.4 1.0
CB B:TRP169 4.7 17.6 1.0
CZ2 B:TRP128 4.7 15.2 1.0
CG B:TRP169 4.8 13.9 1.0
O B:HOH208 4.9 24.5 1.0

Reference:

J.R.Salvador, M.M.Whittaker, J.W.Whittaker, G.B.Jameson. Azide Adduct of the Y174F Mutant of Manganese Superoxide Dismutase From Escherichia Coli To Be Published.
Page generated: Sat Oct 5 13:17:47 2024

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