Zinc in PDB 8q58: Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn
Protein crystallography data
The structure of Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn, PDB code: 8q58
was solved by
M.Sharma,
G.J.Davies,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
63.01 /
1.70
|
Space group
|
I 2 2 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
60.332,
88.49,
126.805,
90,
90,
90
|
R / Rfree (%)
|
18.5 /
20.1
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn
(pdb code 8q58). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the
Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn, PDB code: 8q58:
Jump to Zinc binding site number:
1;
2;
Zinc binding site 1 out
of 2 in 8q58
Go back to
Zinc Binding Sites List in 8q58
Zinc binding site 1 out
of 2 in the Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn
 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 Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn301
b:26.0
occ:0.80
|
OE1
|
A:GLU134
|
1.9
|
27.6
|
1.0
|
NE2
|
A:HIS83
|
2.1
|
25.6
|
0.8
|
NE2
|
A:HIS180
|
2.2
|
49.0
|
1.0
|
ND1
|
A:HIS208
|
2.2
|
20.1
|
0.5
|
CE1
|
A:HIS83
|
2.3
|
25.1
|
0.2
|
O
|
A:HOH434
|
2.6
|
32.2
|
1.0
|
CD
|
A:GLU134
|
2.7
|
31.8
|
1.0
|
OE2
|
A:GLU134
|
2.8
|
32.8
|
1.0
|
NE2
|
A:HIS83
|
2.8
|
25.1
|
0.2
|
CD2
|
A:HIS208
|
2.9
|
42.8
|
0.5
|
CD2
|
A:HIS180
|
2.9
|
61.4
|
1.0
|
CE1
|
A:HIS208
|
3.0
|
23.5
|
0.5
|
CE1
|
A:HIS83
|
3.0
|
27.8
|
0.8
|
CD2
|
A:HIS83
|
3.2
|
25.8
|
0.8
|
CE1
|
A:HIS180
|
3.3
|
34.3
|
1.0
|
CG
|
A:HIS208
|
3.3
|
33.8
|
0.5
|
NE2
|
A:HIS208
|
3.4
|
38.5
|
0.5
|
ZN
|
A:ZN302
|
3.4
|
34.9
|
0.2
|
CG
|
A:HIS208
|
3.4
|
21.2
|
0.5
|
ND1
|
A:HIS83
|
3.5
|
25.0
|
0.2
|
CB
|
A:HIS208
|
3.9
|
29.2
|
0.5
|
CB
|
A:HIS208
|
3.9
|
23.3
|
0.5
|
ND1
|
A:HIS208
|
3.9
|
38.2
|
0.5
|
CE1
|
A:HIS208
|
3.9
|
34.0
|
0.5
|
CG
|
A:HIS180
|
4.1
|
63.5
|
1.0
|
CG
|
A:GLU134
|
4.2
|
26.8
|
1.0
|
CD2
|
A:HIS83
|
4.2
|
25.3
|
0.2
|
O
|
A:HOH445
|
4.2
|
32.8
|
1.0
|
ND1
|
A:HIS83
|
4.2
|
27.5
|
0.8
|
NE2
|
A:HIS208
|
4.2
|
17.5
|
0.5
|
ND1
|
A:HIS180
|
4.3
|
51.9
|
1.0
|
CG
|
A:HIS83
|
4.3
|
25.2
|
0.8
|
O
|
A:HOH515
|
4.3
|
42.5
|
1.0
|
CD2
|
A:HIS208
|
4.4
|
18.8
|
0.5
|
CE
|
A:MET102
|
4.4
|
26.3
|
1.0
|
CG
|
A:HIS83
|
4.4
|
23.9
|
0.2
|
OD2
|
A:ASP104
|
4.5
|
26.6
|
1.0
|
O
|
A:HOH435
|
4.5
|
36.7
|
1.0
|
CB
|
A:GLU134
|
4.8
|
23.4
|
1.0
|
CG
|
A:ASP104
|
5.0
|
26.5
|
1.0
|
|
Zinc binding site 2 out
of 2 in 8q58
Go back to
Zinc Binding Sites List in 8q58
Zinc binding site 2 out
of 2 in the Crystal Structure of Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn
 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 Metal-Dependent Classii Sulfofructosephosphate Aldolase (Sfpa) From Hafnia Paralvei Hpsqia-Zn within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn302
b:34.9
occ:0.20
|
NE2
|
A:HIS83
|
1.8
|
25.1
|
0.2
|
CE1
|
A:HIS83
|
1.9
|
27.8
|
0.8
|
NE2
|
A:HIS83
|
2.6
|
25.6
|
0.8
|
CD2
|
A:HIS83
|
2.7
|
25.3
|
0.2
|
ND1
|
A:HIS208
|
2.8
|
38.2
|
0.5
|
ND1
|
A:HIS83
|
2.9
|
27.5
|
0.8
|
CE1
|
A:HIS83
|
3.0
|
25.1
|
0.2
|
CG
|
A:HIS208
|
3.1
|
33.8
|
0.5
|
ND1
|
A:HIS208
|
3.2
|
20.1
|
0.5
|
CG
|
A:HIS208
|
3.2
|
21.2
|
0.5
|
CD2
|
A:HIS180
|
3.3
|
61.4
|
1.0
|
CB
|
A:HIS208
|
3.3
|
23.3
|
0.5
|
CB
|
A:HIS208
|
3.3
|
29.2
|
0.5
|
ZN
|
A:ZN301
|
3.4
|
26.0
|
0.8
|
O
|
A:HOH452
|
3.4
|
42.0
|
1.0
|
O
|
A:HOH441
|
3.4
|
49.1
|
1.0
|
O
|
A:HOH516
|
3.5
|
56.9
|
1.0
|
CE1
|
A:HIS208
|
3.5
|
34.0
|
0.5
|
NE2
|
A:HIS180
|
3.6
|
49.0
|
1.0
|
CD2
|
A:HIS83
|
3.7
|
25.8
|
0.8
|
CG
|
A:HIS83
|
3.8
|
25.2
|
0.8
|
O
|
A:HOH513
|
3.9
|
44.8
|
1.0
|
CE1
|
A:HIS208
|
3.9
|
23.5
|
0.5
|
CG
|
A:HIS83
|
3.9
|
23.9
|
0.2
|
CD2
|
A:HIS208
|
3.9
|
42.8
|
0.5
|
CD2
|
A:HIS208
|
3.9
|
18.8
|
0.5
|
ND1
|
A:HIS83
|
4.0
|
25.0
|
0.2
|
NE2
|
A:HIS208
|
4.1
|
38.5
|
0.5
|
ND2
|
A:ASN230
|
4.2
|
28.5
|
1.0
|
NE2
|
A:HIS208
|
4.3
|
17.5
|
0.5
|
CA
|
A:HIS208
|
4.3
|
26.9
|
0.5
|
CA
|
A:HIS208
|
4.3
|
24.7
|
0.5
|
CG
|
A:HIS180
|
4.5
|
63.5
|
1.0
|
OD1
|
A:ASP82
|
4.5
|
27.7
|
1.0
|
CE1
|
A:HIS180
|
4.8
|
34.3
|
1.0
|
O
|
A:HOH515
|
5.0
|
42.5
|
1.0
|
OD2
|
A:ASP82
|
5.0
|
33.6
|
1.0
|
N
|
A:GLY209
|
5.0
|
34.7
|
1.0
|
|
Reference:
M.Sharma,
A.Kaur,
N.M.Soler,
J.P.Lingford,
R.Epa,
E.D.Goddard-Borger,
G.J.Davies,
S.J.Williams.
Defining the Molecular Architecture, Metal Dependence, and Distribution of Metal-Dependent Class II Sulfofructose-1-Phosphate Aldolases. J.Biol.Chem. 05338 2023.
ISSN: ESSN 1083-351X
PubMed: 37838169
DOI: 10.1016/J.JBC.2023.105338
Page generated: Thu Oct 31 09:57:13 2024
|