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Magnesium in PDB 1luc: Bacterial Luciferase

Enzymatic activity of Bacterial Luciferase

All present enzymatic activity of Bacterial Luciferase:
1.14.14.3;

Protein crystallography data

The structure of Bacterial Luciferase, PDB code: 1luc was solved by A.J.Fisher, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 150.500, 59.000, 76.500, 90.00, 93.86, 90.00
R / Rfree (%) 18.2 / n/a

Magnesium Binding Sites:

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

Magnesium binding site 1 out of 3 in 1luc

Go back to Magnesium Binding Sites List in 1luc
Magnesium binding site 1 out of 3 in the Bacterial Luciferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Bacterial Luciferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2001

b:28.1
occ:1.00
O A:HOH3174 2.0 22.9 1.0
O A:HOH3177 2.0 19.1 1.0
O A:HOH3175 2.0 25.1 1.0
O A:HOH3176 2.1 21.8 1.0
O A:HOH3101 2.2 19.5 1.0
OE2 A:GLU19 2.3 32.0 1.0
CD A:GLU19 3.2 16.9 1.0
OE1 A:GLU19 3.5 19.0 1.0
O A:HOH3532 4.1 44.2 1.0
O A:HOH3186 4.2 21.7 1.0
O A:HOH3292 4.4 27.5 1.0
CG A:GLU19 4.5 14.1 1.0
O A:HOH3440 4.8 37.4 1.0

Magnesium binding site 2 out of 3 in 1luc

Go back to Magnesium Binding Sites List in 1luc
Magnesium binding site 2 out of 3 in the Bacterial Luciferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Bacterial Luciferase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg2003

b:38.0
occ:1.00
O A:HOH3419 2.0 40.1 1.0
O A:HOH3380 2.1 34.8 1.0
O A:HOH3352 2.1 32.8 1.0
O A:HOH3335 2.1 38.3 1.0
O A:HOH3418 2.2 31.9 1.0
O A:HOH3486 2.4 61.2 1.0
NZ A:LYS2 4.0 0.0 1.0
O A:LYS221 4.0 25.3 1.0
C A:LYS221 4.1 15.3 1.0
O A:HOH3659 4.2 44.9 1.0
O A:HOH3660 4.2 52.8 1.0
O A:THR220 4.2 27.7 1.0
CA A:LYS221 4.2 15.7 1.0
OD1 A:ASP321 4.3 21.6 1.0
OD2 A:ASP321 4.3 60.3 1.0
O A:ILE222 4.5 17.7 1.0
O A:HOH3454 4.6 39.3 1.0
OD1 A:ASP223 4.6 20.4 1.0
C A:ILE222 4.6 20.3 1.0
CA A:ASP223 4.7 14.5 1.0
CG A:ASP321 4.7 28.4 1.0
N A:ASP223 4.7 19.0 1.0
N A:ILE222 4.8 16.7 1.0
O A:HOH3230 4.9 25.9 1.0

Magnesium binding site 3 out of 3 in 1luc

Go back to Magnesium Binding Sites List in 1luc
Magnesium binding site 3 out of 3 in the Bacterial Luciferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Bacterial Luciferase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg2002

b:20.9
occ:1.00
O B:HOH3178 2.0 24.4 1.0
O B:HOH3151 2.1 21.3 1.0
O B:HOH3179 2.1 21.3 1.0
O B:HOH3152 2.2 18.3 1.0
OE1 B:GLU237 2.3 19.6 1.0
CD B:GLU237 3.3 25.5 1.0
OE2 B:GLU237 3.6 21.9 1.0
O B:HOH3592 4.1 64.0 1.0
O B:HOH3095 4.3 18.8 1.0
O B:HOH3511 4.4 40.9 1.0
CG B:GLU237 4.6 13.7 1.0

Reference:

A.J.Fisher, T.B.Thompson, J.B.Thoden, T.O.Baldwin, I.Rayment. The 1.5-A Resolution Crystal Structure of Bacterial Luciferase in Low Salt Conditions. J.Biol.Chem. V. 271 21956 1996.
ISSN: ISSN 0021-9258
PubMed: 8703001
DOI: 10.1074/JBC.271.36.21956
Page generated: Tue Aug 13 08:35:04 2024

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