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Manganese in PDB 3auz: Crystal Structure of MRE11 with Manganese

Protein crystallography data

The structure of Crystal Structure of MRE11 with Manganese, PDB code: 3auz was solved by Y.B.Park, Y.Cho, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.05 / 3.21
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 101.980, 101.980, 113.020, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 26.3

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of MRE11 with Manganese (pdb code 3auz). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Crystal Structure of MRE11 with Manganese, PDB code: 3auz:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in 3auz

Go back to Manganese Binding Sites List in 3auz
Manganese binding site 1 out of 2 in the Crystal Structure of MRE11 with Manganese


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 MRE11 with Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn401

b:0.6
occ:1.00
OD2 A:ASP8 2.3 95.7 1.0
NE2 A:HIS10 2.3 97.6 1.0
OD1 A:ASP49 2.3 97.6 1.0
NE2 A:HIS188 2.3 0.3 1.0
CE1 A:HIS10 3.0 90.0 1.0
CE1 A:HIS188 3.2 0.9 1.0
CG A:ASP49 3.3 84.2 1.0
CD2 A:HIS188 3.4 0.9 1.0
CG A:ASP8 3.4 97.5 1.0
MN A:MN402 3.5 0.2 1.0
CD2 A:HIS10 3.5 91.3 1.0
CB A:ASP49 3.5 82.2 1.0
CB A:ASP8 3.8 94.4 1.0
ND1 A:HIS10 4.2 86.9 1.0
ND1 A:HIS188 4.3 0.5 1.0
CE1 A:HIS158 4.3 92.8 1.0
CA A:ASP8 4.4 86.3 1.0
OD2 A:ASP49 4.4 74.0 1.0
CG A:HIS188 4.4 0.6 1.0
OD1 A:ASP8 4.4 0.1 1.0
CG A:HIS10 4.5 91.9 1.0
NE2 A:HIS158 4.6 94.6 1.0
CA A:HIS186 4.6 0.6 1.0

Manganese binding site 2 out of 2 in 3auz

Go back to Manganese Binding Sites List in 3auz
Manganese binding site 2 out of 2 in the Crystal Structure of MRE11 with Manganese


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 MRE11 with Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn402

b:0.2
occ:1.00
OD1 A:ASN84 2.3 94.7 1.0
OD1 A:ASP49 2.3 97.6 1.0
ND1 A:HIS186 2.3 0.9 1.0
NE2 A:HIS158 2.3 94.6 1.0
CE1 A:HIS186 3.0 0.7 1.0
CE1 A:HIS158 3.1 92.8 1.0
CG A:ASN84 3.2 86.8 1.0
CG A:ASP49 3.2 84.2 1.0
CG A:HIS186 3.4 99.9 1.0
CD2 A:HIS158 3.4 90.2 1.0
MN A:MN401 3.5 0.6 1.0
ND2 A:ASN84 3.5 92.9 1.0
OD2 A:ASP49 3.7 74.0 1.0
CB A:HIS186 3.9 94.6 1.0
CA A:HIS186 4.1 0.6 1.0
NE2 A:HIS186 4.2 0.2 1.0
ND1 A:HIS158 4.3 90.9 1.0
CB A:ASP49 4.3 82.2 1.0
CD2 A:HIS186 4.4 0.7 1.0
OD2 A:ASP8 4.4 95.7 1.0
CG A:HIS158 4.5 89.0 1.0
N A:ASN84 4.5 84.3 1.0
CB A:ASN84 4.6 77.6 1.0
CD2 A:HIS85 4.8 80.2 1.0
O A:HIS186 4.8 98.0 1.0
C A:HIS186 5.0 0.0 1.0

Reference:

H.S.Lim, J.S.Kim, Y.B.Park, G.H.Gwon, Y.Cho. Crystal Structure of the MRE11-RAD50-Atp S Complex: Understanding the Interplay Between MRE11 and RAD50 To Be Published.
Page generated: Tue Dec 15 04:07:46 2020

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