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Magnesium in PDB 3aqn: Complex Structure of Bacterial Protein (Apo Form II)

Enzymatic activity of Complex Structure of Bacterial Protein (Apo Form II)

All present enzymatic activity of Complex Structure of Bacterial Protein (Apo Form II):
2.7.7.19;

Protein crystallography data

The structure of Complex Structure of Bacterial Protein (Apo Form II), PDB code: 3aqn was solved by Y.Toh, D.Takeshita, K.Tomita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.61 / 3.30
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 132.400, 132.400, 176.291, 90.00, 90.00, 90.00
R / Rfree (%) 25.1 / 27.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Complex Structure of Bacterial Protein (Apo Form II) (pdb code 3aqn). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Complex Structure of Bacterial Protein (Apo Form II), PDB code: 3aqn:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 3aqn

Go back to Magnesium Binding Sites List in 3aqn
Magnesium binding site 1 out of 2 in the Complex Structure of Bacterial Protein (Apo Form II)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Complex Structure of Bacterial Protein (Apo Form II) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg600

b:0.3
occ:1.00
OE1 A:GLU108 2.7 0.1 1.0
OE2 A:GLU108 2.7 0.0 1.0
O1A A:ATP501 2.8 0.0 1.0
CD A:GLU108 3.0 0.5 1.0
OD2 A:ASP71 3.5 0.3 1.0
PA A:ATP501 3.7 0.1 1.0
O2A A:ATP501 3.9 0.2 1.0
O5' A:ATP501 4.2 0.8 1.0
CG A:GLU108 4.5 0.7 1.0
CG A:ASP71 4.6 0.5 1.0

Magnesium binding site 2 out of 2 in 3aqn

Go back to Magnesium Binding Sites List in 3aqn
Magnesium binding site 2 out of 2 in the Complex Structure of Bacterial Protein (Apo Form II)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Complex Structure of Bacterial Protein (Apo Form II) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:93.2
occ:1.00
O5' B:ATP502 2.9 0.5 1.0
O1A B:ATP502 3.1 0.6 1.0
PA B:ATP502 3.2 0.3 1.0
O2A B:ATP502 3.2 0.1 1.0
O4' B:ATP502 4.0 0.9 1.0
C5' B:ATP502 4.0 0.8 1.0
C4' B:ATP502 4.4 0.6 1.0
OE1 B:GLU108 4.4 0.5 1.0
O3A B:ATP502 4.8 0.3 1.0

Reference:

Y.Toh, D.Takeshita, T.Nagaike, T.Numata, K.Tomita. Mechanism For the Alteration of the Substrate Specificities of Template-Independent Rna Polymerases Structure V. 19 232 2011.
ISSN: ISSN 0969-2126
PubMed: 21300291
DOI: 10.1016/J.STR.2010.12.006
Page generated: Mon Dec 14 07:53:58 2020

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