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Magnesium in PDB 1o6y: Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis

Enzymatic activity of Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis

All present enzymatic activity of Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis:
2.7.11.1;

Protein crystallography data

The structure of Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis, PDB code: 1o6y was solved by M.Ortiz-Lombardia, F.Pompeo, B.Boitel, P.M.Alzari, Tb Structural Genomicsconsortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 61.00 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 114.607, 122.088, 46.975, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 23

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis (pdb code 1o6y). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis, PDB code: 1o6y:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 1o6y

Go back to Magnesium Binding Sites List in 1o6y
Magnesium binding site 1 out of 2 in the Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1280

b:39.8
occ:1.00
O1A A:ACP1279 2.0 22.4 1.0
O A:HOH2080 2.0 39.3 1.0
O1B A:ACP1279 2.1 24.4 1.0
OD1 A:ASP156 2.1 25.2 1.0
O A:HOH2079 2.1 34.4 1.0
OD1 A:ASN143 2.3 20.5 1.0
CG A:ASP156 3.2 24.8 1.0
PA A:ACP1279 3.2 26.2 1.0
PB A:ACP1279 3.3 28.6 1.0
CG A:ASN143 3.3 23.6 1.0
O3A A:ACP1279 3.5 27.6 1.0
CB A:ASP156 3.6 22.6 1.0
ND2 A:ASN143 3.6 20.2 1.0
O2B A:ACP1279 3.9 27.4 1.0
O A:HOH2055 4.0 38.4 1.0
O2A A:ACP1279 4.2 25.8 1.0
OD2 A:ASP156 4.2 20.6 1.0
O5' A:ACP1279 4.2 25.9 1.0
C5' A:ACP1279 4.5 26.8 1.0
O A:HOH2001 4.6 47.1 1.0
O A:ALA142 4.6 26.9 1.0
CB A:ASN143 4.6 24.8 1.0
C3B A:ACP1279 4.7 25.4 1.0
OD1 A:ASP138 4.8 32.3 1.0
CA A:ASN143 5.0 25.2 1.0

Magnesium binding site 2 out of 2 in 1o6y

Go back to Magnesium Binding Sites List in 1o6y
Magnesium binding site 2 out of 2 in the Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Catalytic Domain of Pknb Kinase From Mycobacterium Tuberculosis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1281

b:45.5
occ:1.00
O A:HOH2054 1.9 35.7 1.0
O2B A:ACP1279 1.9 27.4 1.0
O A:HOH2081 2.1 39.3 1.0
O A:HOH2082 2.1 43.4 1.0
O1G A:ACP1279 2.1 28.4 1.0
O A:HOH2055 2.1 38.4 1.0
PB A:ACP1279 3.1 28.6 1.0
PG A:ACP1279 3.3 27.0 1.0
O1B A:ACP1279 3.6 24.4 1.0
C3B A:ACP1279 3.6 25.4 1.0
NZ A:LYS40 3.7 27.7 1.0
OD2 A:ASP156 3.8 20.6 1.0
OD1 A:ASP156 4.1 25.2 1.0
O A:HOH2085 4.2 61.8 1.0
O3G A:ACP1279 4.2 27.0 1.0
OG A:SER23 4.3 26.3 1.0
CG A:ASP156 4.4 24.8 1.0
O3A A:ACP1279 4.4 27.6 1.0
O2G A:ACP1279 4.4 29.8 1.0
OE1 A:GLU59 4.4 28.7 1.0
O A:HOH2057 4.5 42.4 1.0
O A:HOH2048 4.5 42.3 1.0
CG A:MET22 4.6 31.7 1.0
CE A:MET22 4.6 36.0 1.0
CA A:GLY158 4.9 22.0 1.0
O A:HOH2011 5.0 37.8 1.0
CE A:LYS40 5.0 31.0 1.0

Reference:

M.Ortiz-Lombardia, F.Pompeo, B.Boitel, P.M.Alzari. Crystal Structure of the Catalytic Domain of the Pknb Serine/Threonine Kinase From Mycobacterium Tuberculosis J.Biol.Chem. V. 278 13094 2003.
ISSN: ISSN 0021-9258
PubMed: 12551895
DOI: 10.1074/JBC.M300660200
Page generated: Mon Dec 14 06:34:22 2020

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