Atomistry » Manganese » PDB 1ss9-1uvi » 1txo
Atomistry »
  Manganese »
    PDB 1ss9-1uvi »
      1txo »

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

Go back to Manganese Binding Sites List in 1txo
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

Go back to Manganese Binding Sites List in 1txo
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

Go back to Manganese Binding Sites List in 1txo
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

Go back to Manganese Binding Sites List in 1txo
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

Go back to Manganese Binding Sites List in 1txo
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

Go back to Manganese Binding Sites List in 1txo
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

Last articles

Cl in 5UZH
Cl in 5UZ8
Cl in 5UY1
Cl in 5UXZ
Cl in 5UXE
Cl in 5UXO
Cl in 5UXD
Cl in 5UXN
Cl in 5UX9
Cl in 5UXM
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy