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Magnesium in PDB 1k5p: Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution

Enzymatic activity of Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution

All present enzymatic activity of Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution:
3.8.1.5;

Protein crystallography data

The structure of Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution, PDB code: 1k5p was solved by V.A.Streltsov, J.Damborsky, M.C.J.Wilce, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.77 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.286, 68.369, 80.746, 90.00, 90.00, 90.00
R / Rfree (%) 16.6 / 22.6

Other elements in 1k5p:

The structure of Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution (pdb code 1k5p). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution, PDB code: 1k5p:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 1k5p

Go back to Magnesium Binding Sites List in 1k5p
Magnesium binding site 1 out of 3 in the Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1003

b:19.3
occ:1.00
O A:HOH1297 2.0 14.6 1.0
O A:HOH1164 2.1 21.9 1.0
O A:HOH1170 2.1 14.7 1.0
O A:HOH1314 2.1 15.4 1.0
O A:HOH1214 2.2 12.8 1.0
O A:HOH1298 2.3 20.5 1.0
OE1 A:GLU145 4.1 32.6 1.0
O A:ASP142 4.1 14.6 1.0
OG1 A:THR250 4.1 13.0 1.0
O A:HOH1159 4.2 13.9 1.0
OE2 A:GLU145 4.2 27.2 1.0
O A:HOH1267 4.3 34.7 1.0
O A:HOH1423 4.3 71.7 1.0
O A:HOH1051 4.4 14.7 1.0
CD A:GLU145 4.5 34.0 1.0
O A:ALA141 4.6 16.3 1.0
C A:ASP142 4.6 11.8 1.0
O A:PHE143 4.6 19.7 1.0
CA A:GLY251 4.8 11.4 1.0
N A:GLY251 4.9 13.9 1.0
CA A:ASP142 4.9 12.1 1.0

Magnesium binding site 2 out of 3 in 1k5p

Go back to Magnesium Binding Sites List in 1k5p
Magnesium binding site 2 out of 3 in the Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1004

b:11.5
occ:1.00
O A:HOH1168 2.1 14.2 1.0
O A:HOH1151 2.1 9.3 1.0
O A:HOH1242 2.1 11.7 1.0
O A:HOH1021 2.1 12.6 1.0
O A:HOH1150 2.1 13.5 1.0
O A:HOH1241 2.1 10.9 1.0
O A:HOH1077 4.2 23.7 1.0
OE2 A:GLU192 4.2 13.8 1.0
OD1 A:ASP68 4.2 12.6 1.0
O A:HOH1253 4.3 20.2 1.0
OE1 A:GLU192 4.3 20.6 1.0
O A:GLY67 4.4 7.3 1.0
O A:HOH1121 4.4 17.0 1.0
O A:HOH1011 4.4 10.8 1.0
O A:HOH1394 4.5 44.0 1.0
O A:HOH1230 4.6 39.1 1.0
CD A:GLU192 4.7 18.6 1.0
CA A:ASP68 4.9 12.1 1.0
O A:HOH1092 4.9 25.8 1.0

Magnesium binding site 3 out of 3 in 1k5p

Go back to Magnesium Binding Sites List in 1k5p
Magnesium binding site 3 out of 3 in the Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Hydrolytic Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26 at 1.8A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1005

b:18.0
occ:1.00
O A:HOH1301 2.0 22.1 1.0
O A:HOH1071 2.1 19.7 1.0
O A:HOH1083 2.1 13.0 1.0
O A:HOH1304 2.2 17.9 1.0
O A:HOH1244 2.2 17.8 1.0
O A:HOH1065 2.4 19.0 1.0
O A:HOH1210 3.8 19.7 1.0
OD2 A:ASP70 4.1 12.2 1.0
O A:HOH1023 4.1 9.9 1.0
O A:HOH1091 4.1 15.2 1.0
OE2 A:GLU15 4.2 14.3 1.0
OE1 A:GLU15 4.3 23.1 1.0
O A:GLY18 4.3 12.1 1.0
CD A:GLU15 4.7 22.6 1.0
O A:HOH1371 4.8 39.6 1.0
CB A:ARG20 4.9 19.5 1.0
N A:ARG20 4.9 9.8 1.0

Reference:

V.A.Streltsov, Z.Prokop, J.Damborsky, Y.Nagata, A.Oakley, M.C.J.Wilce. Haloalkane Dehalogenase Linb From Sphingomonas Paucimobilis UT26: X-Ray Crystallographic Studies of Dehalogenation of Brominated Substrates Biochemistry V. 42 10104 2003.
ISSN: ISSN 0006-2960
PubMed: 12939138
DOI: 10.1021/BI027280A
Page generated: Tue Aug 13 07:07:17 2024

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