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Magnesium in PDB 4ch6: Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Propargyloxycarbonyl Lysine

Enzymatic activity of Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Propargyloxycarbonyl Lysine

All present enzymatic activity of Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Propargyloxycarbonyl Lysine:
6.1.1.26;

Protein crystallography data

The structure of Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Propargyloxycarbonyl Lysine, PDB code: 4ch6 was solved by V.Fluegel, M.Vrabel, S.Schneider, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.29 / 2.05
Space group P 64
Cell size a, b, c (Å), α, β, γ (°) 104.933, 104.933, 70.964, 90.00, 90.00, 120.00
R / Rfree (%) 17.369 / 18.474

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Propargyloxycarbonyl Lysine (pdb code 4ch6). 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 Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Propargyloxycarbonyl Lysine, PDB code: 4ch6:

Magnesium binding site 1 out of 1 in 4ch6

Go back to Magnesium Binding Sites List in 4ch6
Magnesium binding site 1 out of 1 in the Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Propargyloxycarbonyl Lysine


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Pyrrolysyl-Trna Synthetase in Complex with Adenylated Propargyloxycarbonyl Lysine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1455

b:80.0
occ:1.00
 O A:HOH2117 2.4 89.1 1.0
OE2 A:GLU396 2.7 52.4 1.0
OAI A:YLA500 2.8 78.3 1.0
OG A:SER399 2.8 71.8 1.0
PBN A:YLA500 3.5 66.0 1.0
CD A:GLU396 3.5 55.5 1.0
OE1 A:GLU396 3.5 59.5 1.0
OAF A:YLA500 3.6 63.8 1.0
O5' A:YLA500 3.7 65.1 1.0
CB A:SER399 3.9 59.6 1.0
C5' A:YLA500 4.6 60.1 1.0
O3' A:YLA500 4.7 48.8 1.0
C3' A:YLA500 4.9 49.8 1.0
CG A:GLU396 4.9 52.1 1.0

Reference:

V.Flugel, M.Vrabel, S.Schneider. Structural Basis For the Site-Specific Incorporation of Lysine Derivatives Into Proteins. Plos One V. 9E96198 2014.
ISSN: ISSN 1932-6203
PubMed: 24760130
DOI: 10.1371/JOURNAL.PONE.0096198
Page generated: Thu Aug 15 16:48:34 2024

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