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Magnesium in PDB 3h08: Crystal Structure of the Ribonuclease H1 From Chlorobium Tepidum

Enzymatic activity of Crystal Structure of the Ribonuclease H1 From Chlorobium Tepidum

All present enzymatic activity of Crystal Structure of the Ribonuclease H1 From Chlorobium Tepidum:
3.1.26.4;

Protein crystallography data

The structure of Crystal Structure of the Ribonuclease H1 From Chlorobium Tepidum, PDB code: 3h08 was solved by K.Ratcliff, J.Corn, S.Marqusee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.60
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 33.457, 33.388, 66.072, 100.38, 99.43, 90.82
R / Rfree (%) 16 / 19.4

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Ribonuclease H1 From Chlorobium Tepidum (pdb code 3h08). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the Ribonuclease H1 From Chlorobium Tepidum, PDB code: 3h08:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3h08

Go back to Magnesium Binding Sites List in 3h08
Magnesium binding site 1 out of 2 in the Crystal Structure of the Ribonuclease H1 From Chlorobium Tepidum


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 the Ribonuclease H1 From Chlorobium Tepidum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:41.1
occ:1.00
O A:HOH212 1.9 34.9 1.0
O A:HOH173 2.6 35.7 1.0
O A:HOH147 2.8 21.5 1.0
O A:HOH200 3.2 49.4 1.0
CG A:GLU48 3.4 25.5 1.0
OG A:SER69 3.5 25.2 1.0
N A:GLY11 3.5 25.4 1.0
CA A:ASP10 3.5 25.3 1.0
CB A:SER71 3.8 21.3 1.0
O A:THR9 3.8 28.5 1.0
N A:SER71 3.8 22.6 1.0
CB A:GLU48 3.9 23.4 1.0
C A:ASP10 3.9 24.9 1.0
N A:ASP70 4.0 24.9 1.0
CA A:GLU48 4.1 23.4 1.0
N A:ASP10 4.3 25.5 1.0
CA A:SER71 4.3 22.1 1.0
CD A:GLU48 4.3 27.3 1.0
CG A:ASP10 4.4 32.2 1.0
C A:THR9 4.4 26.0 1.0
C A:ASP70 4.4 24.2 1.0
CB A:ASP10 4.5 26.3 1.0
CA A:ASP70 4.5 25.1 1.0
CB A:ASP70 4.6 25.8 1.0
O A:GLY11 4.6 29.5 1.0
CA A:GLY11 4.6 25.5 1.0
OD2 A:ASP10 4.7 41.4 1.0
CB A:SER69 4.7 24.1 1.0
OD1 A:ASP10 4.7 44.1 1.0
OE2 A:GLU48 4.8 34.9 1.0
O A:GLU48 4.8 24.0 1.0
OG A:SER71 4.9 21.5 1.0
C A:SER69 4.9 23.9 1.0
CA A:SER69 4.9 23.5 1.0
OG1 A:THR9 5.0 27.7 1.0
C A:GLU48 5.0 24.0 1.0

Magnesium binding site 2 out of 2 in 3h08

Go back to Magnesium Binding Sites List in 3h08
Magnesium binding site 2 out of 2 in the Crystal Structure of the Ribonuclease H1 From Chlorobium Tepidum


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Ribonuclease H1 From Chlorobium Tepidum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:37.7
occ:1.00
O B:HOH181 1.7 46.0 1.0
O B:HOH147 2.8 20.9 1.0
O B:HOH196 2.9 32.9 1.0
CG B:GLU48 3.1 27.0 1.0
OD1 B:ASP70 3.1 39.6 1.0
N B:GLY11 3.4 24.9 1.0
OD1 B:ASP10 3.4 37.5 1.0
CA B:ASP10 3.5 24.2 1.0
CB B:GLU48 3.6 26.8 1.0
OG B:SER69 3.8 20.6 1.0
CA B:GLU48 3.8 25.6 1.0
CB B:SER71 3.9 24.9 1.0
C B:ASP10 3.9 24.9 1.0
O B:THR9 4.0 25.4 1.0
N B:SER71 4.2 24.4 1.0
CD B:GLU48 4.2 30.6 1.0
CG B:ASP10 4.3 30.9 1.0
CG B:ASP70 4.3 28.1 1.0
N B:ASP10 4.3 24.6 1.0
O B:GLY11 4.4 29.1 1.0
C B:THR9 4.4 24.0 1.0
CB B:ASP10 4.4 25.6 1.0
CA B:GLY11 4.4 25.8 1.0
CA B:SER71 4.5 24.5 1.0
N B:ASP70 4.5 23.4 1.0
O B:GLU48 4.6 26.6 1.0
OE2 B:GLU48 4.7 36.1 1.0
C B:GLU48 4.7 25.1 1.0
C B:ASP70 4.8 23.4 1.0
OG B:SER71 4.9 26.1 1.0
N B:GLU48 4.9 23.2 1.0
O B:HOH206 4.9 44.6 1.0
C B:GLY11 4.9 25.8 1.0
O B:HOH237 4.9 38.9 1.0
CB B:SER69 4.9 22.1 1.0
OG1 B:THR9 5.0 26.6 1.0
OD2 B:ASP70 5.0 36.8 1.0
O B:ASP10 5.0 24.2 1.0

Reference:

K.Ratcliff, J.Corn, S.Marqusee. Structure, Stability, and Folding of Ribonuclease H1 From the Moderately Thermophilic Chlorobium Tepidum: Comparison with Thermophilic and Mesophilic Homologues. Biochemistry V. 48 5890 2009.
ISSN: ISSN 0006-2960
PubMed: 19408959
DOI: 10.1021/BI900305P
Page generated: Mon Dec 14 08:12:47 2020

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