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Magnesium in PDB 3hl8: Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp

Enzymatic activity of Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp

All present enzymatic activity of Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp:
3.1.11.1;

Protein crystallography data

The structure of Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp, PDB code: 3hl8 was solved by K.A.Satyshur, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.91 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.823, 91.966, 106.280, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 20.7

Other elements in 3hl8:

The structure of Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp (pdb code 3hl8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp, PDB code: 3hl8:

Magnesium binding site 1 out of 1 in 3hl8

Go back to Magnesium Binding Sites List in 3hl8
Magnesium binding site 1 out of 1 in the Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Exonuclease I in Complex with Inhibitor Bcbp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg500

b:16.4
occ:1.00
 H2 A:HOH519 1.1 17.0 0.0
H1 A:HOH522 1.4 20.8 0.0
H1 A:HOH514 1.7 15.9 0.0
O A:HOH522 2.0 20.8 1.0
OD1 A:ASP15 2.0 17.3 1.0
O A:HOH514 2.1 16.1 1.0
O A:HOH519 2.1 16.9 1.0
O A:HOH520 2.1 19.9 1.0
O A:HOH521 2.1 18.3 1.0
H1 A:HOH520 2.2 19.8 0.0
H2 A:HOH514 2.2 15.9 0.0
H2 A:HOH521 2.4 18.0 0.0
H2 A:HOH522 2.4 20.8 0.0
H1 A:HOH519 2.4 17.0 0.0
H1 A:HOH521 2.9 18.0 0.0
CG A:ASP15 3.1 15.3 1.0
H2 A:HOH520 3.1 19.8 0.0
OD2 A:ASP15 3.4 19.4 1.0
H2 A:HOH512 3.4 15.4 0.0
H1 A:HOH637 3.7 38.1 0.0
H2 A:HOH687 3.8 27.2 0.0
H1 A:HOH711 3.8 33.6 0.0
H1 A:HOH1004 3.8 46.9 0.0
O A:HOH1004 3.9 48.3 1.0
O A:HOH687 3.9 27.6 1.0
OD1 A:ASP108 4.0 15.1 1.0
H1 A:HOH687 4.0 27.2 0.0
O A:TYR16 4.0 15.0 1.0
H2 A:HOH513 4.1 20.0 0.0
O A:HOH512 4.1 15.5 1.0
OD2 A:ASP108 4.1 15.6 1.0
H2 A:HOH637 4.2 38.1 0.0
O A:TYR102 4.2 13.3 1.0
O A:HOH513 4.2 19.8 1.0
O A:HOH637 4.3 38.8 1.0
OD1 A:ASP186 4.3 28.8 1.0
H A:TYR16 4.3 13.4 1.0
O A:HOH711 4.3 33.9 1.0
CB A:ASP15 4.4 13.6 1.0
HA A:ASP15 4.4 13.3 1.0
HD2 A:PHE107 4.5 16.8 1.0
CG A:ASP108 4.5 14.9 1.0
HB2 A:ASP15 4.6 13.7 1.0
H2 A:HOH1004 4.8 46.9 0.0
N A:TYR16 4.8 13.4 1.0
HB3 A:ASP186 4.9 21.7 1.0
CA A:ASP15 4.9 13.5 1.0
H1 A:HOH512 4.9 15.4 0.0
HB3 A:ASN103 5.0 12.7 1.0

Reference:

D.Lu, D.A.Bernstein, K.A.Satyshur, J.L.Keck. Small-Molecule Tools For Dissecting the Roles of Ssb/Protein Interactions in Genome Maintenance Proc.Natl.Acad.Sci.Usa V. 107 633 2010.
ISSN: ISSN 0027-8424
PubMed: 20018747
DOI: 10.1073/PNAS.0909191107
Page generated: Mon Dec 14 08:13:49 2020

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