Calcium in PDB 6iyg: The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose
Enzymatic activity of The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose
All present enzymatic activity of The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose:
3.2.1.60;
Protein crystallography data
The structure of The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose, PDB code: 6iyg
was solved by
Z.F.Li,
X.F.Ban,
Z.Q.Zhang,
C.M.Li,
Z.B.Gu,
T.C.Jin,
Y.L.Li,
Y.H.Shang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
42.44 /
1.50
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
46.280,
64.570,
168.910,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
16.7 /
18.6
|
Calcium Binding Sites:
The binding sites of Calcium atom in the The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose
(pdb code 6iyg). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the
The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose, PDB code: 6iyg:
Jump to Calcium binding site number:
1;
2;
Calcium binding site 1 out
of 2 in 6iyg
Go back to
Calcium Binding Sites List in 6iyg
Calcium binding site 1 out
of 2 in the The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca602
b:25.9
occ:1.00
|
OD1
|
A:ASP1
|
2.1
|
41.2
|
1.0
|
OE1
|
A:GLU17
|
2.2
|
28.9
|
1.0
|
OD1
|
A:ASP16
|
2.3
|
23.6
|
1.0
|
O
|
A:GLN2
|
2.3
|
30.0
|
1.0
|
O
|
A:HIS13
|
2.4
|
25.8
|
1.0
|
ND1
|
A:HIS13
|
2.5
|
25.3
|
1.0
|
CG
|
A:ASP1
|
3.2
|
39.3
|
1.0
|
CG
|
A:ASP16
|
3.4
|
31.1
|
1.0
|
CE1
|
A:HIS13
|
3.4
|
31.4
|
1.0
|
CD
|
A:GLU17
|
3.4
|
29.0
|
1.0
|
C
|
A:HIS13
|
3.4
|
25.9
|
1.0
|
HE1
|
A:HIS13
|
3.4
|
37.7
|
1.0
|
HB3
|
A:HIS13
|
3.5
|
31.8
|
1.0
|
C
|
A:GLN2
|
3.5
|
36.8
|
1.0
|
OD2
|
A:ASP1
|
3.6
|
47.8
|
1.0
|
HG2
|
A:GLU17
|
3.6
|
27.1
|
1.0
|
CG
|
A:HIS13
|
3.6
|
25.6
|
1.0
|
HZ1
|
A:LYS108
|
3.6
|
50.0
|
1.0
|
HA3
|
A:GLY14
|
3.7
|
32.0
|
1.0
|
OD2
|
A:ASP16
|
3.7
|
33.7
|
1.0
|
H
|
A:GLN2
|
3.8
|
45.3
|
1.0
|
HA
|
A:ALA3
|
3.8
|
36.4
|
1.0
|
H
|
A:ASP16
|
3.8
|
29.5
|
1.0
|
CB
|
A:HIS13
|
3.9
|
26.5
|
1.0
|
N
|
A:GLN2
|
4.0
|
37.7
|
1.0
|
HZ3
|
A:LYS108
|
4.0
|
50.0
|
1.0
|
CG
|
A:GLU17
|
4.1
|
22.5
|
1.0
|
NZ
|
A:LYS108
|
4.2
|
41.6
|
1.0
|
N
|
A:GLY14
|
4.3
|
23.7
|
1.0
|
CA
|
A:HIS13
|
4.3
|
26.8
|
1.0
|
CA
|
A:GLN2
|
4.3
|
39.8
|
1.0
|
HA
|
A:ASP1
|
4.3
|
47.3
|
1.0
|
OE2
|
A:GLU17
|
4.3
|
28.0
|
1.0
|
CA
|
A:GLY14
|
4.4
|
26.6
|
1.0
|
C
|
A:ASP1
|
4.4
|
42.2
|
1.0
|
HE2
|
A:LYS108
|
4.4
|
40.7
|
1.0
|
N
|
A:ALA3
|
4.4
|
34.9
|
1.0
|
CB
|
A:ASP1
|
4.5
|
41.5
|
1.0
|
O
|
A:HOH979
|
4.5
|
39.7
|
1.0
|
HG3
|
A:GLU17
|
4.5
|
27.1
|
1.0
|
HB3
|
A:GLN2
|
4.6
|
53.1
|
1.0
|
NE2
|
A:HIS13
|
4.6
|
32.1
|
1.0
|
CA
|
A:ALA3
|
4.6
|
30.3
|
1.0
|
N
|
A:ASP16
|
4.6
|
24.6
|
1.0
|
CA
|
A:ASP1
|
4.7
|
39.4
|
1.0
|
CD2
|
A:HIS13
|
4.7
|
29.5
|
1.0
|
CB
|
A:ASP16
|
4.7
|
24.1
|
1.0
|
HA
|
A:HIS13
|
4.8
|
32.2
|
1.0
|
H
|
A:GLY15
|
4.8
|
28.3
|
1.0
|
N
|
A:GLU17
|
4.8
|
22.6
|
1.0
|
C
|
A:ASP16
|
4.8
|
23.4
|
1.0
|
HB2
|
A:HIS13
|
4.9
|
31.8
|
1.0
|
C
|
A:GLY14
|
4.9
|
26.2
|
1.0
|
H
|
A:GLU17
|
4.9
|
27.1
|
1.0
|
HA
|
A:GLU17
|
4.9
|
24.3
|
1.0
|
HB2
|
A:ASP1
|
4.9
|
49.9
|
1.0
|
HZ2
|
A:LYS108
|
4.9
|
50.0
|
1.0
|
CE
|
A:LYS108
|
4.9
|
33.9
|
1.0
|
CA
|
A:ASP16
|
5.0
|
22.7
|
1.0
|
|
Calcium binding site 2 out
of 2 in 6iyg
Go back to
Calcium Binding Sites List in 6iyg
Calcium binding site 2 out
of 2 in the The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose
Mono view
Stereo pair view
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of The Structure of Maltooligosaccharide-Forming Amylase From Pseudomonas Saccharophila STB07 with Maltotetraose within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca603
b:23.3
occ:1.00
|
O
|
A:HOH739
|
2.3
|
24.5
|
1.0
|
O
|
A:GLY197
|
2.3
|
23.4
|
1.0
|
O
|
A:ASP154
|
2.3
|
23.9
|
1.0
|
OD1
|
A:ASN116
|
2.4
|
22.8
|
1.0
|
OD2
|
A:ASP151
|
2.4
|
24.5
|
1.0
|
OD2
|
A:ASP162
|
2.6
|
25.3
|
1.0
|
OD1
|
A:ASP151
|
2.6
|
23.6
|
1.0
|
CG
|
A:ASP151
|
2.8
|
24.0
|
1.0
|
C
|
A:GLY197
|
3.3
|
21.4
|
1.0
|
HA
|
A:ARG155
|
3.4
|
31.1
|
1.0
|
CG
|
A:ASN116
|
3.4
|
21.2
|
1.0
|
HB3
|
A:ASP162
|
3.5
|
29.4
|
1.0
|
HA2
|
A:GLY197
|
3.5
|
28.1
|
1.0
|
HA3
|
A:GLY197
|
3.5
|
28.1
|
1.0
|
C
|
A:ASP154
|
3.6
|
24.1
|
1.0
|
CG
|
A:ASP162
|
3.6
|
24.3
|
1.0
|
CA
|
A:GLY197
|
3.7
|
23.4
|
1.0
|
ND2
|
A:ASN116
|
3.9
|
23.5
|
1.0
|
HH11
|
A:ARG137
|
4.0
|
31.4
|
1.0
|
CB
|
A:ASP162
|
4.1
|
24.5
|
1.0
|
HD21
|
A:ASN116
|
4.2
|
28.2
|
1.0
|
H
|
A:GLY153
|
4.2
|
30.5
|
1.0
|
HD22
|
A:ASN116
|
4.2
|
28.2
|
1.0
|
O
|
A:GLY153
|
4.2
|
25.8
|
1.0
|
CA
|
A:ARG155
|
4.2
|
25.9
|
1.0
|
C
|
A:GLY153
|
4.2
|
25.1
|
1.0
|
HD2
|
A:ARG137
|
4.3
|
31.9
|
1.0
|
N
|
A:ARG155
|
4.3
|
24.2
|
1.0
|
CB
|
A:ASP151
|
4.3
|
25.5
|
1.0
|
N
|
A:ASP154
|
4.4
|
23.7
|
1.0
|
HA3
|
A:GLY153
|
4.4
|
31.1
|
1.0
|
O
|
A:ASN116
|
4.4
|
23.4
|
1.0
|
O
|
A:HOH746
|
4.4
|
24.5
|
1.0
|
HD1
|
A:TYR198
|
4.5
|
26.4
|
1.0
|
HA
|
A:ASN116
|
4.6
|
25.1
|
1.0
|
N
|
A:TYR198
|
4.6
|
23.0
|
1.0
|
HB3
|
A:TYR198
|
4.6
|
26.1
|
1.0
|
CA
|
A:ASP154
|
4.6
|
22.1
|
1.0
|
HB2
|
A:ASP151
|
4.6
|
30.6
|
1.0
|
HE2
|
A:PHE194
|
4.6
|
30.7
|
1.0
|
O
|
A:LEU163
|
4.7
|
27.1
|
1.0
|
HB2
|
A:ASP162
|
4.7
|
29.4
|
1.0
|
HA
|
A:TYR198
|
4.7
|
27.0
|
1.0
|
CB
|
A:ASN116
|
4.7
|
24.5
|
1.0
|
CA
|
A:GLY153
|
4.7
|
25.9
|
1.0
|
OD1
|
A:ASP162
|
4.7
|
28.4
|
1.0
|
NH1
|
A:ARG137
|
4.7
|
26.1
|
1.0
|
H
|
A:ASP154
|
4.7
|
28.5
|
1.0
|
HB3
|
A:ASP151
|
4.8
|
30.6
|
1.0
|
N
|
A:GLY153
|
4.8
|
25.4
|
1.0
|
HH12
|
A:ARG137
|
4.9
|
31.4
|
1.0
|
HB2
|
A:ARG137
|
4.9
|
33.0
|
1.0
|
HB3
|
A:ARG155
|
4.9
|
29.4
|
1.0
|
HA
|
A:ASP162
|
5.0
|
29.4
|
1.0
|
HB2
|
A:ASN116
|
5.0
|
29.4
|
1.0
|
|
Reference:
Z.Q.Zhang,
X.F.Ban,
Z.F.Li,
T.C.Jin,
Y.L.Li,
Z.B.Gu,
C.M.Li,
Y.H.Shang.
Maltotetraose-Forming Amylase From Pseudomonas Saccharophila STB07 To Be Published.
Page generated: Tue Jul 16 09:37:38 2024
|