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Manganese in PDB 1txo: Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A.

Enzymatic activity of Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A.

All present enzymatic activity of Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A.:
3.1.3.16;

Protein crystallography data

The structure of Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A., PDB code: 1txo was solved by K.E.Pullen, H.L.Ng, P.Y.Sung, M.C.Good, S.M.Smith, T.Alber, Tb Structuralgenomics Consortium (Tbsgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 72.55 / 1.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 67.638, 58.757, 73.815, 90.00, 102.15, 90.00
R / Rfree (%) 19.9 / 23

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A. (pdb code 1txo). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 6 binding sites of Manganese where determined in the Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A., PDB code: 1txo:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6;

Manganese binding site 1 out of 6 in 1txo

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Manganese binding site 1 out of 6 in the Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn700

b:22.1
occ:1.00
 OD2 A:ASP229 2.1 26.1 1.0
O A:HOH831 2.1 20.5 1.0
OD1 A:ASP191 2.2 21.4 1.0
OD2 A:ASP38 2.2 22.3 1.0
O A:HOH726 2.2 21.8 1.0
O A:HOH705 2.2 22.5 1.0
CG A:ASP38 3.1 20.4 1.0
CG A:ASP229 3.1 28.2 1.0
CG A:ASP191 3.2 23.9 1.0
OD1 A:ASP38 3.3 18.8 1.0
OD1 A:ASP229 3.4 25.9 1.0
OD2 A:ASP191 3.5 24.3 1.0
MN A:MN701 3.8 26.9 1.0
O A:HOH723 3.9 28.1 1.0
O A:HOH727 4.1 37.0 1.0
O A:HOH714 4.2 27.1 1.0
O A:HOH704 4.2 15.7 1.0
O A:HOH721 4.3 24.6 1.0
N A:GLY192 4.3 22.8 1.0
O A:HOH724 4.4 17.6 1.0
O A:ASN230 4.4 25.0 1.0
CB A:ASP229 4.5 29.2 1.0
CB A:ASP38 4.5 20.7 1.0
OD1 A:ASP25 4.5 22.8 1.0
CB A:ASP191 4.5 22.7 1.0
N A:ASP191 4.6 21.9 1.0
C A:ASP191 4.8 22.8 1.0
CB A:SER190 4.8 20.6 1.0
CA A:ASP191 4.8 22.6 1.0
O A:HOH812 4.9 56.8 1.0
OG A:SER190 4.9 20.4 1.0
CA A:GLY192 5.0 23.2 1.0

Manganese binding site 2 out of 6 in 1txo

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Manganese binding site 2 out of 6 in the Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn701

b:26.9
occ:1.00
 OD1 A:ASP38 2.1 18.8 1.0
O A:GLY39 2.2 22.6 1.0
O A:HOH723 2.2 28.1 1.0
O A:HOH831 2.3 20.5 1.0
O A:HOH724 2.4 17.6 1.0
O A:HOH715 2.4 24.1 1.0
CG A:ASP38 3.3 20.4 1.0
C A:GLY39 3.4 23.6 1.0
OD2 A:ASP38 3.8 22.3 1.0
MN A:MN700 3.8 22.1 1.0
N A:GLY39 3.8 22.2 1.0
C A:ASP38 4.1 21.6 1.0
O A:HOH727 4.1 37.0 1.0
O A:HOH722 4.2 32.0 1.0
CA A:GLY39 4.2 22.9 1.0
OD1 A:ASP25 4.2 22.8 1.0
O A:HOH726 4.3 21.8 1.0
CB A:GLU24 4.3 25.5 1.0
N A:MSE40 4.3 25.1 1.0
OD1 A:ASN230 4.4 24.4 1.0
O A:HOH804 4.4 46.2 1.0
O A:HOH725 4.4 32.5 1.0
O A:HOH705 4.5 22.5 1.0
O A:ASP38 4.5 21.2 1.0
OE1 A:GLU24 4.5 31.0 1.0
CA A:MSE40 4.5 26.6 1.0
CB A:ASP38 4.5 20.7 1.0
CA A:ASP38 4.6 20.9 1.0
OD1 A:ASP229 4.6 25.9 1.0
CB A:MSE40 4.8 27.5 1.0
C A:GLU24 4.8 24.1 1.0
O A:GLU24 4.9 23.7 1.0

Manganese binding site 3 out of 6 in 1txo

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Manganese binding site 3 out of 6 in the Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn702

b:24.2
occ:1.00
 OD2 A:ASP118 1.9 23.6 1.0
O A:HOH832 2.0 24.8 1.0
OG A:SER160 2.1 28.8 1.0
O A:SER160 2.1 27.0 1.0
OD2 A:ASP191 2.3 24.3 1.0
O A:HOH707 2.3 31.0 1.0
CG A:ASP118 3.1 24.1 1.0
C A:SER160 3.1 27.6 1.0
CB A:SER160 3.2 28.2 1.0
CG A:ASP191 3.3 23.9 1.0
CA A:SER160 3.4 28.2 1.0
OD1 A:ASP118 3.7 24.1 1.0
CB A:ASP191 3.7 22.7 1.0
O A:HOH721 3.9 24.6 1.0
OD2 A:ASP195 4.0 27.5 1.0
O A:HOH726 4.0 21.8 1.0
CB A:ASP118 4.1 23.3 1.0
O A:HOH717 4.3 23.8 1.0
N A:LEU161 4.3 27.0 1.0
OD1 A:ASP191 4.4 21.4 1.0
OD1 A:ASP195 4.5 27.8 1.0
O A:HOH812 4.7 56.8 1.0
O A:HOH708 4.7 28.1 1.0
CG A:ASP195 4.8 27.9 1.0
N A:ILE162 4.8 27.2 1.0
N A:SER160 4.8 28.6 1.0
CA A:LEU161 4.9 27.1 1.0
C A:LEU161 4.9 27.1 1.0

Manganese binding site 4 out of 6 in 1txo

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Manganese binding site 4 out of 6 in the Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn703

b:32.7
occ:1.00
 OD1 B:ASP38 2.1 21.1 1.0
O B:GLY39 2.3 24.4 1.0
O B:HOH799 2.3 26.7 1.0
O B:HOH725 2.3 24.7 1.0
O B:HOH718 2.4 21.9 1.0
O B:HOH726 2.5 27.5 1.0
CG B:ASP38 3.3 22.2 1.0
C B:GLY39 3.4 25.0 1.0
OD2 B:ASP38 3.7 23.9 1.0
MN B:MN704 3.8 22.4 1.0
N B:GLY39 3.9 23.0 1.0
O B:HOH778 4.0 39.0 1.0
O B:HOH800 4.0 27.3 1.0
O B:HOH727 4.1 33.5 1.0
C B:ASP38 4.1 21.9 1.0
O B:HOH767 4.2 29.1 1.0
CA B:GLY39 4.3 23.8 1.0
OD1 B:ASP25 4.3 21.6 1.0
CB B:GLU24 4.4 29.2 1.0
OE1 B:GLU24 4.4 34.3 1.0
N B:MSE40 4.4 26.4 1.0
O B:ASP38 4.4 21.5 1.0
O B:HOH805 4.5 21.5 1.0
CB B:ASP38 4.5 21.3 1.0
CA B:MSE40 4.6 27.9 1.0
CA B:ASP38 4.6 21.5 1.0
OD1 B:ASN230 4.6 27.1 1.0
O B:HOH728 4.6 37.0 1.0
OD1 B:ASP229 4.7 28.8 1.0
CB B:MSE40 4.8 28.8 1.0
O B:GLU24 4.9 27.1 1.0
C B:GLU24 4.9 27.4 1.0

Manganese binding site 5 out of 6 in 1txo

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Manganese binding site 5 out of 6 in the Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn704

b:22.4
occ:1.00
 O B:HOH805 2.1 21.5 1.0
OD2 B:ASP38 2.1 23.9 1.0
O B:HOH799 2.1 26.7 1.0
O B:HOH800 2.1 27.3 1.0
OD1 B:ASP191 2.2 21.1 1.0
OD2 B:ASP229 2.2 27.5 1.0
CG B:ASP38 3.1 22.2 1.0
CG B:ASP191 3.2 20.9 1.0
CG B:ASP229 3.2 30.0 1.0
OD1 B:ASP38 3.4 21.1 1.0
OD2 B:ASP191 3.5 19.6 1.0
OD1 B:ASP229 3.5 28.8 1.0
MN B:MN703 3.8 32.7 1.0
O B:HOH725 3.9 24.7 1.0
O B:HOH727 4.0 33.5 1.0
O B:HOH706 4.2 16.0 1.0
N B:GLY192 4.2 22.1 1.0
O B:HOH724 4.3 29.3 1.0
O B:HOH707 4.3 20.5 1.0
O B:ASN230 4.4 26.8 1.0
O B:HOH718 4.4 21.9 1.0
OD1 B:ASP25 4.5 21.6 1.0
CB B:ASP38 4.5 21.3 1.0
CB B:ASP191 4.5 21.2 1.0
N B:ASP191 4.6 21.1 1.0
CB B:ASP229 4.6 31.1 1.0
C B:ASP191 4.7 22.0 1.0
CB B:SER190 4.8 21.1 1.0
CA B:ASP191 4.8 21.4 1.0
CA B:GLY192 4.9 22.5 1.0

Manganese binding site 6 out of 6 in 1txo

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Manganese binding site 6 out of 6 in the Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A.


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of the Mycobacterium Tuberculosis Serine/Threonine Phosphatase Pstp/Ppp at 1.95 A. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn705

b:21.9
occ:1.00
 OD2 B:ASP118 2.0 23.1 1.0
OG B:SER160 2.1 26.1 1.0
O B:SER160 2.2 24.1 1.0
O B:HOH798 2.2 27.9 1.0
OD2 B:ASP191 2.2 19.6 1.0
O B:HOH720 2.4 23.4 1.0
C B:SER160 3.1 24.3 1.0
CG B:ASP118 3.2 21.9 1.0
CB B:SER160 3.2 25.1 1.0
CG B:ASP191 3.3 20.9 1.0
CA B:SER160 3.4 25.1 1.0
CB B:ASP191 3.8 21.2 1.0
OD1 B:ASP118 3.8 20.6 1.0
OD2 B:ASP195 4.0 30.3 1.0
O B:HOH707 4.0 20.5 1.0
O B:HOH800 4.1 27.3 1.0
O B:HOH803 4.2 46.9 1.0
CB B:ASP118 4.3 21.4 1.0
OD1 B:ASP191 4.3 21.1 1.0
N B:LEU161 4.4 23.4 1.0
O B:HOH721 4.5 23.8 1.0
OD1 B:ASP195 4.5 26.3 1.0
N B:ILE162 4.7 23.6 1.0
CG B:ASP195 4.7 28.2 1.0
O B:HOH717 4.8 23.4 1.0
N B:SER160 4.8 25.5 1.0
C B:LEU161 4.9 23.1 1.0
CA B:LEU161 4.9 23.2 1.0
CG2 B:THR137 5.0 24.2 1.0

Reference:

K.E.Pullen, H.L.Ng, P.Y.Sung, M.C.Good, S.M.Smith, T.Alber. An Alternate Conformation and A Third Metal in Pstp/Ppp, the M. Tuberculosis PP2C-Family Ser/Thr Protein Phosphatase. Structure V. 12 1947 2004.
ISSN: ISSN 0969-2126
PubMed: 15530359
DOI: 10.1016/J.STR.2004.09.008
Page generated: Sat Oct 5 12:37:09 2024

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