Zinc in PDB 2f3d: Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase
Enzymatic activity of Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase
All present enzymatic activity of Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase:
3.1.3.11;
Protein crystallography data
The structure of Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase, PDB code: 2f3d
was solved by
C.V.Iancu,
S.Mukund,
J.-Y.Choe,
H.J.Fromm,
R.B.Honzatko,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
5.00 /
1.83
|
Space group
|
I 2 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
55.840,
82.502,
165.025,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.2 /
24.6
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase
(pdb code 2f3d). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the
Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase, PDB code: 2f3d:
Jump to Zinc binding site number:
1;
2;
3;
Zinc binding site 1 out
of 3 in 2f3d
Go back to
Zinc Binding Sites List in 2f3d
Zinc binding site 1 out
of 3 in the Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn340
b:30.6
occ:1.00
|
OE1
|
A:GLU97
|
2.1
|
27.6
|
1.0
|
OD2
|
A:ASP118
|
2.2
|
13.8
|
1.0
|
O4
|
A:PO4434
|
2.4
|
14.5
|
1.0
|
O
|
A:HOH511
|
2.4
|
20.4
|
1.0
|
O
|
A:LEU120
|
2.4
|
14.8
|
1.0
|
O2
|
A:PO4434
|
2.4
|
14.7
|
1.0
|
P
|
A:PO4434
|
2.9
|
13.7
|
1.0
|
CD
|
A:GLU97
|
3.2
|
26.7
|
1.0
|
CG
|
A:ASP118
|
3.3
|
14.4
|
1.0
|
C
|
A:LEU120
|
3.3
|
15.2
|
1.0
|
ZN
|
A:ZN341
|
3.7
|
15.2
|
1.0
|
OD1
|
A:ASP118
|
3.7
|
14.2
|
1.0
|
OE2
|
A:GLU98
|
3.9
|
34.5
|
1.0
|
ZN
|
A:ZN342
|
3.9
|
36.7
|
1.0
|
O3
|
A:PO4434
|
3.9
|
14.8
|
1.0
|
O
|
A:HOH519
|
3.9
|
27.3
|
1.0
|
O1
|
A:PO4434
|
4.0
|
14.1
|
1.0
|
OE2
|
A:GLU97
|
4.0
|
26.2
|
1.0
|
CA
|
A:ASP121
|
4.0
|
13.9
|
1.0
|
N
|
A:ASP121
|
4.0
|
14.8
|
1.0
|
CG
|
A:GLU97
|
4.1
|
26.7
|
1.0
|
N
|
A:LEU120
|
4.1
|
15.3
|
1.0
|
O
|
A:HOH624
|
4.2
|
25.2
|
1.0
|
CB
|
A:GLU97
|
4.3
|
26.1
|
1.0
|
CA
|
A:LEU120
|
4.3
|
15.6
|
1.0
|
CB
|
A:ASP118
|
4.6
|
14.4
|
1.0
|
CA
|
A:ASP118
|
4.8
|
15.5
|
1.0
|
CD
|
A:PRO119
|
4.8
|
16.8
|
1.0
|
NH2
|
A:ARG276
|
4.8
|
18.8
|
1.0
|
CB
|
A:ASP121
|
4.8
|
13.8
|
1.0
|
C
|
A:ASP118
|
4.9
|
15.8
|
1.0
|
CB
|
A:LEU120
|
4.9
|
17.1
|
1.0
|
OD2
|
A:ASP74
|
4.9
|
31.1
|
1.0
|
N
|
A:PRO119
|
4.9
|
16.4
|
1.0
|
CG
|
A:PRO119
|
5.0
|
17.1
|
1.0
|
CD
|
A:GLU98
|
5.0
|
33.8
|
1.0
|
|
Zinc binding site 2 out
of 3 in 2f3d
Go back to
Zinc Binding Sites List in 2f3d
Zinc binding site 2 out
of 3 in the Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn341
b:15.2
occ:1.00
|
O2
|
A:PO4434
|
1.9
|
14.7
|
1.0
|
OD1
|
A:ASP118
|
1.9
|
14.2
|
1.0
|
OD1
|
A:ASP121
|
2.0
|
14.2
|
1.0
|
OE1
|
A:GLU280
|
2.0
|
14.4
|
1.0
|
CG
|
A:ASP121
|
2.9
|
14.0
|
1.0
|
CG
|
A:ASP118
|
2.9
|
14.4
|
1.0
|
CD
|
A:GLU280
|
3.1
|
14.6
|
1.0
|
CB
|
A:ASP121
|
3.2
|
13.8
|
1.0
|
P
|
A:PO4434
|
3.2
|
13.7
|
1.0
|
OD2
|
A:ASP118
|
3.3
|
13.8
|
1.0
|
CG
|
A:GLU280
|
3.5
|
14.5
|
1.0
|
CA
|
A:ASP121
|
3.5
|
13.9
|
1.0
|
O1
|
A:PO4434
|
3.6
|
14.1
|
1.0
|
ZN
|
A:ZN340
|
3.7
|
30.6
|
1.0
|
NH2
|
A:ARG276
|
3.8
|
18.8
|
1.0
|
O3
|
A:PO4434
|
3.9
|
14.8
|
1.0
|
OD2
|
A:ASP121
|
4.1
|
12.9
|
1.0
|
C1
|
A:F6P339
|
4.1
|
14.7
|
1.0
|
O3
|
A:F6P339
|
4.2
|
13.3
|
1.0
|
OE2
|
A:GLU280
|
4.2
|
15.4
|
1.0
|
CB
|
A:ASP118
|
4.2
|
14.4
|
1.0
|
O4
|
A:PO4434
|
4.3
|
14.5
|
1.0
|
N
|
A:GLY122
|
4.4
|
14.4
|
1.0
|
C
|
A:ASP121
|
4.5
|
14.0
|
1.0
|
N
|
A:ASP121
|
4.5
|
14.8
|
1.0
|
O
|
A:LEU120
|
4.6
|
14.8
|
1.0
|
C3
|
A:F6P339
|
4.7
|
14.7
|
1.0
|
CD1
|
A:ILE135
|
4.7
|
12.1
|
1.0
|
OE1
|
A:GLU97
|
4.7
|
27.6
|
1.0
|
C2
|
A:F6P339
|
4.8
|
14.3
|
1.0
|
O2
|
A:F6P339
|
4.9
|
14.1
|
1.0
|
O1
|
A:F6P339
|
4.9
|
14.2
|
1.0
|
C
|
A:LEU120
|
4.9
|
15.2
|
1.0
|
CZ
|
A:ARG276
|
5.0
|
19.3
|
1.0
|
CB
|
A:GLU280
|
5.0
|
14.4
|
1.0
|
|
Zinc binding site 3 out
of 3 in 2f3d
Go back to
Zinc Binding Sites List in 2f3d
Zinc binding site 3 out
of 3 in the Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase
 Mono view
 Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Fructose-1,6-Bisphosphatase within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn342
b:36.7
occ:1.00
|
O3
|
A:PO4434
|
2.1
|
14.8
|
1.0
|
O
|
A:HOH624
|
2.1
|
25.2
|
1.0
|
OE2
|
A:GLU97
|
2.4
|
26.2
|
1.0
|
O4
|
A:PO4434
|
2.5
|
14.5
|
1.0
|
OD2
|
A:ASP68
|
2.5
|
39.9
|
1.0
|
P
|
A:PO4434
|
2.8
|
13.7
|
1.0
|
CD
|
A:GLU97
|
3.1
|
26.7
|
1.0
|
OE1
|
A:GLU97
|
3.2
|
27.6
|
1.0
|
CG
|
A:ASP68
|
3.2
|
40.0
|
1.0
|
CB
|
A:ASP68
|
3.4
|
40.1
|
1.0
|
O2
|
A:PO4434
|
3.7
|
14.7
|
1.0
|
NH2
|
A:ARG276
|
3.8
|
18.8
|
1.0
|
O
|
A:HOH680
|
3.8
|
19.9
|
1.0
|
ZN
|
A:ZN340
|
3.9
|
30.6
|
1.0
|
ND2
|
A:ASN64
|
4.0
|
44.9
|
1.0
|
O1
|
A:PO4434
|
4.0
|
14.1
|
1.0
|
OE2
|
A:GLU98
|
4.2
|
34.5
|
1.0
|
NH1
|
A:ARG276
|
4.2
|
19.1
|
1.0
|
OD1
|
A:ASP68
|
4.3
|
39.9
|
1.0
|
O1
|
A:F6P339
|
4.3
|
14.2
|
1.0
|
CG
|
A:GLU97
|
4.5
|
26.7
|
1.0
|
CZ
|
A:ARG276
|
4.5
|
19.3
|
1.0
|
CB
|
A:SER123
|
4.6
|
19.4
|
1.0
|
O
|
A:HOH681
|
4.6
|
20.3
|
1.0
|
O
|
A:HOH519
|
4.8
|
27.3
|
1.0
|
CA
|
A:ASP68
|
4.9
|
40.3
|
1.0
|
|
Reference:
Y.Gao,
C.V.Iancu,
S.Mukind,
J.Y.Choe,
R.B.Honzatko.
Mechanism of Displacement of A Catalytically Essential Loop From the Active Site of Mammalian Fructose-1,6-Bisphosphatase. Biochemistry V. 52 5206 2013.
ISSN: ISSN 0006-2960
PubMed: 23844654
DOI: 10.1021/BI400532N
Page generated: Wed Oct 16 23:37:07 2024
|