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
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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
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