Zinc in PDB 1y13: Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps)
Enzymatic activity of Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps)
All present enzymatic activity of Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps):
4.2.3.12;
Protein crystallography data
The structure of Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps), PDB code: 1y13
was solved by
J.Bosch,
W.G.J.Hol,
Structural Genomics Of Pathogenic Protozoaconsortium (Sgpp),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
20.00 /
2.20
|
Space group
|
P 43 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
103.319,
103.319,
131.111,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.5 /
23.5
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps)
(pdb code 1y13). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps), PDB code: 1y13:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 1y13
Go back to
Zinc Binding Sites List in 1y13
Zinc binding site 1 out
of 3 in the Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps)
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn174
b:62.7
occ:1.00
|
O10
|
A:BIO175
|
1.9
|
61.0
|
1.0
|
NE2
|
A:HIS41
|
2.1
|
57.0
|
1.0
|
NE2
|
A:HIS43
|
2.2
|
55.2
|
1.0
|
NE2
|
A:HIS29
|
2.3
|
50.7
|
1.0
|
O9
|
A:BIO175
|
2.3
|
57.6
|
1.0
|
C10
|
A:BIO175
|
3.0
|
76.8
|
1.0
|
CE1
|
A:HIS41
|
3.1
|
55.8
|
1.0
|
CE1
|
A:HIS29
|
3.1
|
52.5
|
1.0
|
CD2
|
A:HIS43
|
3.1
|
48.8
|
1.0
|
CD2
|
A:HIS41
|
3.2
|
54.4
|
1.0
|
C9
|
A:BIO175
|
3.2
|
67.9
|
1.0
|
CE1
|
A:HIS43
|
3.3
|
49.8
|
1.0
|
CD2
|
A:HIS29
|
3.4
|
54.0
|
1.0
|
OE1
|
A:GLU161
|
3.7
|
74.5
|
1.0
|
OE2
|
A:GLU38
|
4.0
|
63.2
|
1.0
|
N5
|
A:BIO175
|
4.1
|
64.7
|
1.0
|
C6
|
A:BIO175
|
4.1
|
57.2
|
1.0
|
ND1
|
A:HIS41
|
4.2
|
54.0
|
1.0
|
CG
|
A:HIS41
|
4.3
|
56.0
|
1.0
|
C11
|
A:BIO175
|
4.3
|
78.4
|
1.0
|
ND1
|
A:HIS29
|
4.3
|
55.0
|
1.0
|
CG
|
A:HIS43
|
4.3
|
52.1
|
1.0
|
CD
|
A:GLU161
|
4.3
|
68.4
|
1.0
|
OE2
|
A:GLU161
|
4.3
|
67.8
|
1.0
|
ND1
|
A:HIS43
|
4.4
|
48.5
|
1.0
|
O
|
A:HOH176
|
4.5
|
42.6
|
1.0
|
CG
|
A:HIS29
|
4.5
|
52.2
|
1.0
|
CD
|
A:GLU38
|
4.8
|
60.5
|
1.0
|
CD1
|
A:ILE31
|
5.0
|
66.4
|
1.0
|
|
Zinc binding site 2 out
of 3 in 1y13
Go back to
Zinc Binding Sites List in 1y13
Zinc binding site 2 out
of 3 in the Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps)
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn174
b:64.7
occ:1.00
|
NE2
|
B:HIS41
|
2.1
|
55.3
|
1.0
|
NE2
|
B:HIS43
|
2.2
|
50.1
|
1.0
|
NE2
|
B:HIS29
|
2.3
|
52.7
|
1.0
|
O9
|
B:BIO175
|
2.4
|
61.1
|
1.0
|
O10
|
B:BIO175
|
2.4
|
63.4
|
1.0
|
C10
|
B:BIO175
|
3.0
|
77.7
|
1.0
|
CE1
|
B:HIS41
|
3.0
|
53.8
|
1.0
|
CD2
|
B:HIS43
|
3.1
|
50.4
|
1.0
|
CE1
|
B:HIS29
|
3.1
|
50.8
|
1.0
|
CD2
|
B:HIS41
|
3.1
|
57.8
|
1.0
|
C9
|
B:BIO175
|
3.2
|
66.4
|
1.0
|
CE1
|
B:HIS43
|
3.3
|
52.8
|
1.0
|
CD2
|
B:HIS29
|
3.4
|
51.1
|
1.0
|
OE1
|
B:GLU161
|
3.7
|
74.6
|
1.0
|
C6
|
B:BIO175
|
4.1
|
57.6
|
1.0
|
OE2
|
B:GLU38
|
4.1
|
62.9
|
1.0
|
ND1
|
B:HIS41
|
4.2
|
55.0
|
1.0
|
N5
|
B:BIO175
|
4.2
|
62.1
|
1.0
|
CG
|
B:HIS41
|
4.3
|
52.1
|
1.0
|
CG
|
B:HIS43
|
4.3
|
51.2
|
1.0
|
ND1
|
B:HIS29
|
4.3
|
53.4
|
1.0
|
CD
|
B:GLU161
|
4.3
|
70.9
|
1.0
|
ND1
|
B:HIS43
|
4.4
|
53.0
|
1.0
|
OE2
|
B:GLU161
|
4.4
|
67.1
|
1.0
|
CG
|
B:HIS29
|
4.4
|
51.1
|
1.0
|
C11
|
B:BIO175
|
4.5
|
77.7
|
1.0
|
O
|
B:HOH177
|
4.5
|
41.6
|
1.0
|
CD1
|
B:ILE31
|
4.9
|
64.7
|
1.0
|
OH
|
B:TYR45
|
5.0
|
55.7
|
1.0
|
|
Zinc binding site 3 out
of 3 in 1y13
Go back to
Zinc Binding Sites List in 1y13
Zinc binding site 3 out
of 3 in the Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps)
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn174
b:65.3
occ:1.00
|
NE2
|
C:HIS43
|
2.2
|
59.7
|
1.0
|
NE2
|
C:HIS29
|
2.3
|
46.2
|
1.0
|
NE2
|
C:HIS41
|
2.4
|
60.3
|
1.0
|
O9
|
C:BIO175
|
2.5
|
64.3
|
1.0
|
O10
|
C:BIO175
|
2.6
|
66.7
|
1.0
|
C10
|
C:BIO175
|
3.0
|
75.7
|
1.0
|
CE1
|
C:HIS29
|
3.1
|
44.7
|
1.0
|
CD2
|
C:HIS43
|
3.1
|
51.1
|
1.0
|
C9
|
C:BIO175
|
3.2
|
63.4
|
1.0
|
CE1
|
C:HIS43
|
3.3
|
53.0
|
1.0
|
CD2
|
C:HIS41
|
3.4
|
58.4
|
1.0
|
CE1
|
C:HIS41
|
3.4
|
56.0
|
1.0
|
CD2
|
C:HIS29
|
3.4
|
50.6
|
1.0
|
OE1
|
C:GLU161
|
3.6
|
76.7
|
1.0
|
N5
|
C:BIO175
|
4.0
|
62.5
|
1.0
|
C6
|
C:BIO175
|
4.1
|
57.6
|
1.0
|
O
|
C:HOH189
|
4.1
|
67.5
|
1.0
|
OE2
|
C:GLU38
|
4.2
|
66.1
|
1.0
|
CD
|
C:GLU161
|
4.3
|
70.2
|
1.0
|
CG
|
C:HIS43
|
4.3
|
54.9
|
1.0
|
ND1
|
C:HIS29
|
4.3
|
56.3
|
1.0
|
ND1
|
C:HIS43
|
4.3
|
57.1
|
1.0
|
OE2
|
C:GLU161
|
4.4
|
68.5
|
1.0
|
ND1
|
C:HIS41
|
4.5
|
57.0
|
1.0
|
CG
|
C:HIS41
|
4.5
|
55.5
|
1.0
|
CG
|
C:HIS29
|
4.5
|
54.5
|
1.0
|
C11
|
C:BIO175
|
4.5
|
77.9
|
1.0
|
OH
|
C:TYR45
|
4.9
|
55.0
|
1.0
|
OE1
|
C:GLU38
|
4.9
|
69.8
|
1.0
|
CD
|
C:GLU38
|
4.9
|
61.8
|
1.0
|
|
Reference:
J.Bosch,
W.G.J.Hol,
Structural Genomics Of Pathogenic Protozoa Consortium (Sgpp).
Structural Analysis of Plasmodium Falciparum 6-Pyruvoyl Tetrahydropterin Synthase (Ptps) To Be Published.
Page generated: Wed Oct 16 20:41:42 2024
|