Zinc in PDB 6igs: Crystal Structure of Hprt From F. Tularensis with Zinc
Enzymatic activity of Crystal Structure of Hprt From F. Tularensis with Zinc
All present enzymatic activity of Crystal Structure of Hprt From F. Tularensis with Zinc:
2.4.2.8;
Protein crystallography data
The structure of Crystal Structure of Hprt From F. Tularensis with Zinc, PDB code: 6igs
was solved by
G.C.Pavithra,
S.V.Kundapura,
U.A.Ramagopal,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
37.24 /
2.16
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
78.764,
90.193,
113.707,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
18.3 /
23.2
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Hprt From F. Tularensis with Zinc
(pdb code 6igs). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 8 binding sites of Zinc where determined in the
Crystal Structure of Hprt From F. Tularensis with Zinc, PDB code: 6igs:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Zinc binding site 1 out
of 8 in 6igs
Go back to
Zinc Binding Sites List in 6igs
Zinc binding site 1 out
of 8 in the Crystal Structure of Hprt From F. Tularensis with Zinc
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure of Hprt From F. Tularensis with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn203
b:32.6
occ:1.00
|
OE2
|
A:GLU102
|
2.0
|
30.3
|
1.0
|
O
|
A:HOH334
|
2.1
|
29.9
|
1.0
|
OD1
|
A:ASP103
|
2.1
|
27.5
|
1.0
|
O
|
A:HOH312
|
2.3
|
34.4
|
1.0
|
O
|
A:HOH305
|
2.3
|
31.9
|
1.0
|
O
|
A:HOH318
|
2.5
|
24.4
|
1.0
|
CD
|
A:GLU102
|
2.8
|
27.9
|
1.0
|
OE1
|
A:GLU102
|
3.0
|
28.6
|
1.0
|
CG
|
A:ASP103
|
3.1
|
24.5
|
1.0
|
OD2
|
A:ASP103
|
3.5
|
27.2
|
1.0
|
O1
|
A:SO4201
|
3.7
|
33.5
|
1.0
|
N
|
A:ASP103
|
4.1
|
20.6
|
1.0
|
CG
|
A:GLU102
|
4.2
|
26.3
|
1.0
|
CB
|
A:ASP103
|
4.4
|
22.2
|
1.0
|
N
|
A:ILE104
|
4.4
|
23.5
|
1.0
|
O
|
A:ILE104
|
4.4
|
23.9
|
1.0
|
CG1
|
A:VAL42
|
4.4
|
17.2
|
1.0
|
OG
|
A:SER46
|
4.5
|
19.2
|
0.5
|
O
|
A:VAL42
|
4.5
|
16.4
|
1.0
|
CA
|
A:ASP103
|
4.7
|
21.9
|
1.0
|
O2
|
A:SO4201
|
4.8
|
43.0
|
1.0
|
CB
|
A:VAL42
|
4.9
|
17.5
|
1.0
|
CB
|
A:GLU102
|
4.9
|
24.9
|
1.0
|
S
|
A:SO4201
|
4.9
|
34.6
|
1.0
|
CG2
|
A:ILE104
|
4.9
|
29.9
|
1.0
|
CA
|
A:GLU102
|
5.0
|
21.3
|
1.0
|
|
Zinc binding site 2 out
of 8 in 6igs
Go back to
Zinc Binding Sites List in 6igs
Zinc binding site 2 out
of 8 in the Crystal Structure of Hprt From F. Tularensis with Zinc
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure of Hprt From F. Tularensis with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn204
b:86.6
occ:1.00
|
ND1
|
A:HIS109
|
1.9
|
56.6
|
1.0
|
OE2
|
A:GLU139
|
1.9
|
55.2
|
1.0
|
NE2
|
A:HIS112
|
2.3
|
57.6
|
1.0
|
CE1
|
A:HIS109
|
2.8
|
57.0
|
1.0
|
CE1
|
A:HIS112
|
2.9
|
55.2
|
1.0
|
CG
|
A:HIS109
|
2.9
|
50.3
|
1.0
|
CD
|
A:GLU139
|
3.0
|
62.9
|
1.0
|
CB
|
A:HIS109
|
3.4
|
44.2
|
1.0
|
OE1
|
A:GLU139
|
3.4
|
59.4
|
1.0
|
CA
|
A:HIS109
|
3.5
|
40.9
|
1.0
|
CD2
|
A:HIS112
|
3.6
|
56.1
|
1.0
|
NE2
|
A:HIS109
|
4.0
|
57.0
|
1.0
|
CD2
|
A:HIS109
|
4.0
|
53.9
|
1.0
|
ND1
|
A:HIS112
|
4.1
|
56.2
|
1.0
|
O
|
A:HIS109
|
4.2
|
38.8
|
1.0
|
NH2
|
A:ARG140
|
4.3
|
91.3
|
1.0
|
CG
|
A:GLU139
|
4.3
|
67.7
|
1.0
|
C
|
A:HIS109
|
4.3
|
40.4
|
1.0
|
CG
|
A:HIS112
|
4.5
|
52.3
|
1.0
|
N
|
A:HIS109
|
4.5
|
38.7
|
1.0
|
CZ
|
A:ARG140
|
4.8
|
89.6
|
1.0
|
NH1
|
A:ARG140
|
4.9
|
84.9
|
1.0
|
|
Zinc binding site 3 out
of 8 in 6igs
Go back to
Zinc Binding Sites List in 6igs
Zinc binding site 3 out
of 8 in the Crystal Structure of Hprt From F. Tularensis with Zinc
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure of Hprt From F. Tularensis with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn202
b:17.3
occ:1.00
|
NE2
|
B:HIS112
|
1.9
|
13.8
|
1.0
|
ND1
|
B:HIS109
|
1.9
|
21.7
|
1.0
|
OE2
|
B:GLU139
|
2.1
|
17.8
|
1.0
|
CE1
|
B:HIS109
|
2.7
|
22.5
|
1.0
|
CD
|
B:GLU139
|
2.8
|
18.8
|
1.0
|
CD2
|
B:HIS112
|
2.8
|
13.5
|
1.0
|
OE1
|
B:GLU139
|
2.9
|
18.2
|
1.0
|
CE1
|
B:HIS112
|
3.0
|
14.3
|
1.0
|
CG
|
B:HIS109
|
3.1
|
20.0
|
1.0
|
CA
|
B:HIS109
|
3.6
|
16.7
|
1.0
|
CB
|
B:HIS109
|
3.6
|
18.1
|
1.0
|
NH1
|
B:ARG140
|
3.7
|
19.7
|
1.0
|
NE2
|
B:HIS109
|
4.0
|
21.9
|
1.0
|
CG
|
B:HIS112
|
4.0
|
13.6
|
1.0
|
ND1
|
B:HIS112
|
4.1
|
14.0
|
1.0
|
CD2
|
B:HIS109
|
4.1
|
21.4
|
1.0
|
O
|
B:HIS109
|
4.2
|
16.7
|
1.0
|
CG
|
B:GLU139
|
4.2
|
19.6
|
1.0
|
C
|
B:HIS109
|
4.4
|
16.6
|
1.0
|
N
|
B:HIS109
|
4.6
|
15.3
|
1.0
|
CZ
|
B:ARG140
|
4.8
|
21.1
|
1.0
|
O
|
B:GLY108
|
4.9
|
14.7
|
1.0
|
CE
|
B:LYS113
|
4.9
|
20.7
|
1.0
|
|
Zinc binding site 4 out
of 8 in 6igs
Go back to
Zinc Binding Sites List in 6igs
Zinc binding site 4 out
of 8 in the Crystal Structure of Hprt From F. Tularensis with Zinc
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure of Hprt From F. Tularensis with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn203
b:37.9
occ:1.00
|
OD1
|
B:ASP103
|
2.2
|
24.7
|
1.0
|
O
|
B:HOH322
|
2.2
|
23.2
|
1.0
|
OE2
|
B:GLU102
|
2.2
|
22.6
|
1.0
|
O
|
B:HOH344
|
2.3
|
34.4
|
1.0
|
O
|
B:HOH335
|
2.5
|
32.0
|
1.0
|
O
|
B:HOH346
|
2.6
|
34.5
|
1.0
|
CD
|
B:GLU102
|
2.9
|
22.0
|
1.0
|
CG
|
B:ASP103
|
3.0
|
20.7
|
1.0
|
OE1
|
B:GLU102
|
3.1
|
23.2
|
1.0
|
OD2
|
B:ASP103
|
3.3
|
24.0
|
1.0
|
N
|
B:ASP103
|
4.0
|
15.8
|
1.0
|
CG
|
B:GLU102
|
4.0
|
22.3
|
1.0
|
OG
|
B:SER46
|
4.2
|
13.0
|
0.5
|
CB
|
B:ASP103
|
4.3
|
18.7
|
1.0
|
N
|
B:ILE104
|
4.4
|
15.7
|
1.0
|
CG1
|
B:VAL42
|
4.4
|
11.5
|
1.0
|
O
|
B:ILE104
|
4.5
|
17.3
|
1.0
|
O
|
B:VAL42
|
4.6
|
11.3
|
1.0
|
CA
|
B:ASP103
|
4.6
|
16.8
|
1.0
|
O
|
B:HOH317
|
4.8
|
23.1
|
1.0
|
CB
|
B:VAL42
|
4.8
|
11.4
|
1.0
|
CA
|
B:GLU102
|
4.9
|
16.3
|
1.0
|
C
|
B:GLU102
|
4.9
|
15.3
|
1.0
|
CG2
|
B:ILE104
|
5.0
|
20.1
|
1.0
|
|
Zinc binding site 5 out
of 8 in 6igs
Go back to
Zinc Binding Sites List in 6igs
Zinc binding site 5 out
of 8 in the Crystal Structure of Hprt From F. Tularensis with Zinc
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Crystal Structure of Hprt From F. Tularensis with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn203
b:35.5
occ:1.00
|
OE1
|
C:GLU102
|
1.9
|
39.7
|
1.0
|
O
|
C:HOH302
|
2.0
|
36.9
|
1.0
|
O
|
C:HOH301
|
2.3
|
23.7
|
1.0
|
OD1
|
C:ASP103
|
2.3
|
25.8
|
1.0
|
O
|
C:HOH322
|
2.3
|
35.7
|
1.0
|
O
|
C:HOH328
|
2.4
|
36.5
|
1.0
|
CD
|
C:GLU102
|
2.8
|
35.3
|
1.0
|
CG
|
C:ASP103
|
3.2
|
23.5
|
1.0
|
OE2
|
C:GLU102
|
3.3
|
36.1
|
1.0
|
OD2
|
C:ASP103
|
3.5
|
26.8
|
1.0
|
O3
|
C:SO4202
|
3.6
|
45.4
|
1.0
|
CG
|
C:GLU102
|
3.8
|
32.1
|
1.0
|
N
|
C:ASP103
|
4.1
|
20.5
|
1.0
|
OG
|
C:SER46
|
4.2
|
19.0
|
0.5
|
O
|
C:ILE104
|
4.3
|
23.2
|
1.0
|
N
|
C:ILE104
|
4.4
|
19.8
|
1.0
|
CG1
|
C:VAL42
|
4.4
|
23.9
|
1.0
|
CB
|
C:ASP103
|
4.5
|
21.4
|
1.0
|
O
|
C:VAL42
|
4.6
|
26.0
|
1.0
|
CG2
|
C:ILE104
|
4.7
|
24.2
|
1.0
|
CA
|
C:ASP103
|
4.8
|
20.7
|
1.0
|
O
|
C:HOH319
|
4.8
|
26.7
|
1.0
|
CB
|
C:GLU102
|
4.9
|
28.2
|
1.0
|
S
|
C:SO4202
|
5.0
|
54.1
|
1.0
|
CB
|
C:VAL42
|
5.0
|
24.9
|
1.0
|
CA
|
C:GLU102
|
5.0
|
24.1
|
1.0
|
|
Zinc binding site 6 out
of 8 in 6igs
Go back to
Zinc Binding Sites List in 6igs
Zinc binding site 6 out
of 8 in the Crystal Structure of Hprt From F. Tularensis with Zinc
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Crystal Structure of Hprt From F. Tularensis with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Zn204
b:36.0
occ:1.00
|
NE2
|
C:HIS112
|
2.0
|
32.8
|
1.0
|
OE2
|
C:GLU139
|
2.1
|
31.6
|
1.0
|
ND1
|
C:HIS109
|
2.1
|
42.3
|
1.0
|
CD
|
C:GLU139
|
2.8
|
29.3
|
1.0
|
CE1
|
C:HIS109
|
2.9
|
44.0
|
1.0
|
CE1
|
C:HIS112
|
3.0
|
35.3
|
1.0
|
CG
|
C:HIS109
|
3.0
|
37.1
|
1.0
|
OE1
|
C:GLU139
|
3.0
|
31.7
|
1.0
|
CD2
|
C:HIS112
|
3.0
|
34.1
|
1.0
|
CB
|
C:HIS109
|
3.4
|
33.2
|
1.0
|
CA
|
C:HIS109
|
3.5
|
30.5
|
1.0
|
NH2
|
C:ARG140
|
3.5
|
46.9
|
1.0
|
NE2
|
C:HIS109
|
4.0
|
42.1
|
1.0
|
CD2
|
C:HIS109
|
4.0
|
40.9
|
1.0
|
ND1
|
C:HIS112
|
4.1
|
34.8
|
1.0
|
CG
|
C:HIS112
|
4.1
|
33.9
|
1.0
|
CG
|
C:GLU139
|
4.2
|
28.5
|
1.0
|
C
|
C:HIS109
|
4.4
|
31.7
|
1.0
|
CZ
|
C:ARG140
|
4.4
|
47.5
|
1.0
|
N
|
C:HIS109
|
4.5
|
28.5
|
1.0
|
O
|
C:HIS109
|
4.5
|
32.1
|
1.0
|
NE
|
C:ARG140
|
4.6
|
44.4
|
1.0
|
|
Zinc binding site 7 out
of 8 in 6igs
Go back to
Zinc Binding Sites List in 6igs
Zinc binding site 7 out
of 8 in the Crystal Structure of Hprt From F. Tularensis with Zinc
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of Crystal Structure of Hprt From F. Tularensis with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn203
b:36.3
occ:1.00
|
OD1
|
D:ASP103
|
2.2
|
30.8
|
1.0
|
OE1
|
D:GLU102
|
2.2
|
34.6
|
1.0
|
O
|
D:HOH309
|
2.3
|
25.2
|
1.0
|
O
|
D:HOH313
|
2.5
|
40.4
|
1.0
|
O
|
D:HOH330
|
2.5
|
32.0
|
1.0
|
O
|
D:HOH334
|
2.6
|
39.2
|
1.0
|
CD
|
D:GLU102
|
2.9
|
30.9
|
1.0
|
CG
|
D:ASP103
|
3.1
|
28.5
|
1.0
|
OE2
|
D:GLU102
|
3.2
|
31.5
|
1.0
|
OD2
|
D:ASP103
|
3.5
|
30.5
|
1.0
|
O2
|
D:SO4202
|
3.9
|
57.8
|
1.0
|
CG
|
D:GLU102
|
4.1
|
29.7
|
1.0
|
N
|
D:ASP103
|
4.1
|
22.6
|
1.0
|
CB
|
D:ASP103
|
4.4
|
26.3
|
1.0
|
O
|
D:ILE104
|
4.5
|
23.9
|
1.0
|
N
|
D:ILE104
|
4.5
|
21.9
|
1.0
|
CG1
|
D:VAL42
|
4.5
|
21.6
|
1.0
|
O
|
D:VAL42
|
4.5
|
18.7
|
1.0
|
CA
|
D:ASP103
|
4.7
|
23.5
|
1.0
|
CG2
|
D:ILE104
|
4.9
|
25.3
|
1.0
|
CB
|
D:VAL42
|
4.9
|
20.4
|
1.0
|
CA
|
D:GLU102
|
5.0
|
24.0
|
1.0
|
|
Zinc binding site 8 out
of 8 in 6igs
Go back to
Zinc Binding Sites List in 6igs
Zinc binding site 8 out
of 8 in the Crystal Structure of Hprt From F. Tularensis with Zinc
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of Crystal Structure of Hprt From F. Tularensis with Zinc within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Zn204
b:30.8
occ:1.00
|
OE1
|
D:GLU139
|
1.8
|
29.8
|
1.0
|
ND1
|
D:HIS109
|
1.9
|
32.0
|
1.0
|
NE2
|
D:HIS112
|
2.0
|
29.9
|
1.0
|
CE1
|
D:HIS109
|
2.8
|
32.5
|
1.0
|
CD
|
D:GLU139
|
2.8
|
31.9
|
1.0
|
CD2
|
D:HIS112
|
3.0
|
28.8
|
1.0
|
CG
|
D:HIS109
|
3.0
|
29.8
|
1.0
|
CE1
|
D:HIS112
|
3.1
|
30.5
|
1.0
|
OE2
|
D:GLU139
|
3.3
|
31.9
|
1.0
|
CB
|
D:HIS109
|
3.5
|
27.3
|
1.0
|
CA
|
D:HIS109
|
3.5
|
26.7
|
1.0
|
NE2
|
D:HIS109
|
4.0
|
32.4
|
1.0
|
CD2
|
D:HIS109
|
4.1
|
30.6
|
1.0
|
CG
|
D:HIS112
|
4.2
|
28.5
|
1.0
|
ND1
|
D:HIS112
|
4.2
|
30.1
|
1.0
|
CG
|
D:GLU139
|
4.2
|
32.1
|
1.0
|
O
|
D:HIS109
|
4.3
|
29.0
|
1.0
|
C
|
D:HIS109
|
4.4
|
27.4
|
1.0
|
N
|
D:HIS109
|
4.6
|
26.3
|
1.0
|
NH2
|
D:ARG140
|
4.8
|
44.9
|
1.0
|
|
Reference:
G.C.Pavithra,
U.A.Ramagopal.
Crystal Structure of Hypoxanthine Phosphoribosyltransferase From Francisella Tularensis To Be Published.
Page generated: Mon Oct 28 23:49:58 2024
|