Zinc in PDB 1fj6: Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)
Enzymatic activity of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)
All present enzymatic activity of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State):
3.1.3.11;
Protein crystallography data
The structure of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State), PDB code: 1fj6
was solved by
C.V.Iancu,
J.Y.Choe,
R.B.Honzatko,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
5.00 /
2.50
|
Space group
|
I 2 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
52.380,
82.470,
165.590,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.3 /
27.2
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)
(pdb code 1fj6). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State), PDB code: 1fj6:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 1fj6
Go back to
Zinc Binding Sites List in 1fj6
Zinc binding site 1 out
of 3 in the Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn403
b:26.3
occ:1.00
|
O
|
A:LEU120
|
2.0
|
14.4
|
1.0
|
OD2
|
A:ASP118
|
2.1
|
28.6
|
1.0
|
OE1
|
A:GLU97
|
2.3
|
15.8
|
1.0
|
O1
|
A:PO4402
|
2.3
|
20.1
|
1.0
|
O3
|
A:PO4402
|
2.5
|
25.0
|
1.0
|
P
|
A:PO4402
|
2.9
|
25.2
|
1.0
|
C
|
A:LEU120
|
3.1
|
17.9
|
1.0
|
CG
|
A:ASP118
|
3.2
|
26.0
|
1.0
|
CD
|
A:GLU97
|
3.2
|
15.1
|
1.0
|
OD1
|
A:ASP118
|
3.6
|
35.5
|
1.0
|
O2
|
A:PO4402
|
3.7
|
21.3
|
1.0
|
N
|
A:LEU120
|
3.8
|
20.1
|
1.0
|
ZN
|
A:ZN404
|
3.9
|
27.7
|
1.0
|
ZN
|
A:ZN405
|
3.9
|
33.8
|
1.0
|
OE2
|
A:GLU97
|
3.9
|
13.7
|
1.0
|
N
|
A:ASP121
|
3.9
|
20.5
|
1.0
|
CA
|
A:LEU120
|
3.9
|
21.0
|
1.0
|
OE1
|
A:GLU98
|
4.0
|
31.5
|
1.0
|
CA
|
A:ASP121
|
4.1
|
21.7
|
1.0
|
O4
|
A:PO4402
|
4.1
|
23.0
|
1.0
|
CG
|
A:GLU97
|
4.2
|
18.1
|
1.0
|
OD2
|
A:ASP74
|
4.3
|
31.2
|
1.0
|
CB
|
A:ASP118
|
4.5
|
24.5
|
1.0
|
CB
|
A:LEU120
|
4.5
|
21.9
|
1.0
|
CD
|
A:PRO119
|
4.6
|
19.2
|
1.0
|
C
|
A:ASP118
|
4.6
|
21.5
|
1.0
|
CA
|
A:ASP118
|
4.6
|
19.8
|
1.0
|
N
|
A:PRO119
|
4.7
|
19.6
|
1.0
|
CB
|
A:GLU97
|
4.8
|
22.4
|
1.0
|
NH2
|
A:ARG276
|
4.9
|
22.7
|
1.0
|
C
|
A:PRO119
|
5.0
|
19.4
|
1.0
|
CB
|
A:ASP121
|
5.0
|
22.2
|
1.0
|
|
Zinc binding site 2 out
of 3 in 1fj6
Go back to
Zinc Binding Sites List in 1fj6
Zinc binding site 2 out
of 3 in the Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn404
b:27.7
occ:1.00
|
OD1
|
A:ASP118
|
1.9
|
35.5
|
1.0
|
O1
|
A:PO4402
|
2.1
|
20.1
|
1.0
|
OD1
|
A:ASP121
|
2.1
|
26.1
|
1.0
|
OE1
|
A:GLU280
|
2.2
|
31.9
|
1.0
|
CG
|
A:ASP118
|
3.0
|
26.0
|
1.0
|
CG
|
A:ASP121
|
3.1
|
28.0
|
1.0
|
CD
|
A:GLU280
|
3.1
|
25.9
|
1.0
|
CB
|
A:ASP121
|
3.3
|
22.2
|
1.0
|
P
|
A:PO4402
|
3.3
|
25.2
|
1.0
|
OD2
|
A:ASP118
|
3.4
|
28.6
|
1.0
|
CA
|
A:ASP121
|
3.5
|
21.7
|
1.0
|
CG
|
A:GLU280
|
3.5
|
23.5
|
1.0
|
O4
|
A:PO4402
|
3.5
|
23.0
|
1.0
|
ZN
|
A:ZN403
|
3.9
|
26.3
|
1.0
|
NH2
|
A:ARG276
|
3.9
|
22.7
|
1.0
|
OE1
|
A:GLU97
|
4.0
|
15.8
|
1.0
|
C1
|
A:F6P401
|
4.1
|
15.9
|
1.0
|
O2
|
A:PO4402
|
4.1
|
21.3
|
1.0
|
CB
|
A:ASP118
|
4.2
|
24.5
|
1.0
|
OD2
|
A:ASP121
|
4.2
|
25.6
|
1.0
|
OE2
|
A:GLU280
|
4.3
|
29.5
|
1.0
|
O
|
A:LEU120
|
4.3
|
14.4
|
1.0
|
O3
|
A:F6P401
|
4.4
|
13.6
|
1.0
|
N
|
A:GLY122
|
4.4
|
20.7
|
1.0
|
O3
|
A:PO4402
|
4.4
|
25.0
|
1.0
|
CD1
|
A:ILE135
|
4.4
|
10.9
|
1.0
|
C
|
A:ASP121
|
4.5
|
22.8
|
1.0
|
N
|
A:ASP121
|
4.5
|
20.5
|
1.0
|
O1
|
A:F6P401
|
4.6
|
16.2
|
1.0
|
O2
|
A:F6P401
|
4.7
|
21.1
|
1.0
|
C2
|
A:F6P401
|
4.8
|
18.7
|
1.0
|
C
|
A:LEU120
|
4.8
|
17.9
|
1.0
|
C3
|
A:F6P401
|
4.8
|
17.7
|
1.0
|
CB
|
A:GLU280
|
4.9
|
18.5
|
1.0
|
CD
|
A:GLU97
|
5.0
|
15.1
|
1.0
|
|
Zinc binding site 3 out
of 3 in 1fj6
Go back to
Zinc Binding Sites List in 1fj6
Zinc binding site 3 out
of 3 in the Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State)
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Fructose-1,6-Bisphosphatase (Mutant Y57W) Product/Zn Complex (R-State) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn405
b:33.8
occ:1.00
|
O2
|
A:PO4402
|
1.9
|
21.3
|
1.0
|
OD2
|
A:ASP68
|
2.2
|
28.3
|
1.0
|
OE2
|
A:GLU97
|
2.4
|
13.7
|
1.0
|
O3
|
A:PO4402
|
2.8
|
25.0
|
1.0
|
P
|
A:PO4402
|
2.9
|
25.2
|
1.0
|
CD
|
A:GLU97
|
3.1
|
15.1
|
1.0
|
CG
|
A:ASP68
|
3.1
|
30.7
|
1.0
|
CB
|
A:ASP68
|
3.4
|
31.8
|
1.0
|
OE1
|
A:GLU97
|
3.5
|
15.8
|
1.0
|
O1
|
A:PO4402
|
3.7
|
20.1
|
1.0
|
ND2
|
A:ASN64
|
3.8
|
28.8
|
1.0
|
NH2
|
A:ARG276
|
3.8
|
22.7
|
1.0
|
ZN
|
A:ZN403
|
3.9
|
26.3
|
1.0
|
OE1
|
A:GLU98
|
3.9
|
31.5
|
1.0
|
O4
|
A:PO4402
|
4.1
|
23.0
|
1.0
|
CG
|
A:GLU97
|
4.2
|
18.1
|
1.0
|
OD1
|
A:ASP68
|
4.3
|
31.5
|
1.0
|
NH1
|
A:ARG276
|
4.3
|
22.3
|
1.0
|
CZ
|
A:ARG276
|
4.6
|
25.5
|
1.0
|
O1
|
A:F6P401
|
4.8
|
16.2
|
1.0
|
CB
|
A:SER123
|
4.8
|
19.8
|
1.0
|
CA
|
A:ASP68
|
5.0
|
35.4
|
1.0
|
OG
|
A:SER123
|
5.0
|
24.3
|
1.0
|
|
Reference:
S.W.Nelson,
C.V.Iancu,
J.Y.Choe,
R.B.Honzatko,
H.J.Fromm.
Tryptophan Fluorescence Reveals the Conformational State of A Dynamic Loop in Recombinant Porcine Fructose-1,6-Bisphosphatase. Biochemistry V. 39 11100 2000.
ISSN: ISSN 0006-2960
PubMed: 10998248
DOI: 10.1021/BI000609C
Page generated: Sun Oct 13 00:57:13 2024
|