Sodium in PDB 8d4i: Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine
Enzymatic activity of Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine
All present enzymatic activity of Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine:
4.1.1.116;
Protein crystallography data
The structure of Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine, PDB code: 8d4i
was solved by
R.S.Phillips,
K.N.Nguyen Hoang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
41.36 /
1.32
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
140.88,
50.44,
139.18,
90,
116.93,
90
|
R / Rfree (%)
|
14.6 /
17.1
|
Other elements in 8d4i:
The structure of Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine
(pdb code 8d4i). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the
Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine, PDB code: 8d4i:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 8d4i
Go back to
Sodium Binding Sites List in 8d4i
Sodium binding site 1 out
of 2 in the Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 1 of Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na509
b:19.7
occ:1.00
|
O
|
A:HOH1058
|
2.3
|
54.7
|
1.0
|
O
|
A:VAL210
|
2.4
|
19.1
|
1.0
|
O
|
A:MET207
|
2.5
|
21.6
|
1.0
|
O
|
A:ILE204
|
2.5
|
17.8
|
1.0
|
O
|
A:HOH1026
|
2.9
|
24.4
|
1.0
|
O
|
A:LEU205
|
3.0
|
27.2
|
1.0
|
HA
|
A:LEU205
|
3.1
|
24.0
|
1.0
|
C
|
A:LEU205
|
3.5
|
21.4
|
1.0
|
H
|
A:MET207
|
3.5
|
22.8
|
1.0
|
C
|
A:MET207
|
3.6
|
20.7
|
1.0
|
C
|
A:VAL210
|
3.6
|
14.9
|
1.0
|
C
|
A:ILE204
|
3.6
|
19.4
|
1.0
|
CA
|
A:LEU205
|
3.7
|
20.0
|
1.0
|
HB2
|
A:MET207
|
3.7
|
23.7
|
1.0
|
H
|
A:VAL210
|
3.7
|
19.3
|
1.0
|
HA
|
A:HIS211
|
3.8
|
18.8
|
1.0
|
N
|
A:MET207
|
3.8
|
18.9
|
1.0
|
HG22
|
A:ILE204
|
4.0
|
21.4
|
1.0
|
N
|
A:LEU205
|
4.1
|
19.9
|
1.0
|
CA
|
A:MET207
|
4.1
|
17.6
|
1.0
|
HB
|
A:VAL210
|
4.1
|
17.9
|
1.0
|
HG23
|
A:ILE204
|
4.2
|
21.4
|
1.0
|
O
|
A:HOH1025
|
4.3
|
36.0
|
1.0
|
O
|
A:HOH934
|
4.3
|
42.8
|
1.0
|
N
|
A:ALA206
|
4.4
|
20.5
|
1.0
|
N
|
A:VAL210
|
4.4
|
16.1
|
1.0
|
CB
|
A:MET207
|
4.4
|
19.8
|
1.0
|
CA
|
A:VAL210
|
4.5
|
14.5
|
1.0
|
H
|
A:LEU212
|
4.5
|
18.8
|
1.0
|
N
|
A:HIS211
|
4.5
|
15.4
|
1.0
|
CG2
|
A:ILE204
|
4.5
|
17.8
|
1.0
|
C
|
A:ALA206
|
4.6
|
22.5
|
1.0
|
CA
|
A:HIS211
|
4.6
|
15.6
|
1.0
|
HA
|
A:PRO208
|
4.6
|
23.4
|
1.0
|
N
|
A:PRO208
|
4.7
|
19.2
|
1.0
|
HD23
|
A:LEU205
|
4.8
|
34.7
|
1.0
|
HB3
|
A:MET207
|
4.8
|
23.7
|
1.0
|
CB
|
A:VAL210
|
4.8
|
14.9
|
1.0
|
CA
|
A:ILE204
|
4.9
|
17.4
|
1.0
|
O
|
A:HOH986
|
4.9
|
37.9
|
1.0
|
HA
|
A:ILE204
|
4.9
|
20.9
|
1.0
|
H
|
A:ALA206
|
4.9
|
24.7
|
1.0
|
C
|
A:PRO208
|
4.9
|
20.9
|
1.0
|
H
|
A:LEU205
|
5.0
|
23.9
|
1.0
|
CA
|
A:PRO208
|
5.0
|
19.5
|
1.0
|
CA
|
A:ALA206
|
5.0
|
22.4
|
1.0
|
|
Sodium binding site 2 out
of 2 in 8d4i
Go back to
Sodium Binding Sites List in 8d4i
Sodium binding site 2 out
of 2 in the Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine
Mono view
Stereo pair view
|
A full contact list of Sodium with other atoms in the Na binding
site number 2 of Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with Putrescine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Na505
b:18.4
occ:1.00
|
O
|
C:VAL210
|
2.4
|
19.8
|
1.0
|
O
|
C:HOH1069
|
2.4
|
54.8
|
1.0
|
O
|
C:MET207
|
2.5
|
20.1
|
1.0
|
O
|
C:ILE204
|
2.6
|
19.1
|
1.0
|
O
|
C:HOH1058
|
2.9
|
25.0
|
1.0
|
O
|
C:LEU205
|
3.0
|
30.0
|
1.0
|
HA
|
C:LEU205
|
3.1
|
29.1
|
1.0
|
C
|
C:LEU205
|
3.4
|
23.9
|
1.0
|
H
|
C:MET207
|
3.5
|
22.3
|
1.0
|
C
|
C:VAL210
|
3.6
|
16.9
|
1.0
|
CA
|
C:LEU205
|
3.6
|
24.2
|
1.0
|
C
|
C:MET207
|
3.6
|
21.3
|
1.0
|
HB2
|
C:MET207
|
3.6
|
22.7
|
1.0
|
C
|
C:ILE204
|
3.7
|
17.8
|
1.0
|
HA
|
C:HIS211
|
3.8
|
19.8
|
1.0
|
N
|
C:MET207
|
3.8
|
18.6
|
1.0
|
H
|
C:VAL210
|
3.8
|
19.0
|
1.0
|
HG22
|
C:ILE204
|
4.0
|
19.5
|
1.0
|
N
|
C:LEU205
|
4.1
|
21.3
|
1.0
|
CA
|
C:MET207
|
4.2
|
17.6
|
1.0
|
HB
|
C:VAL210
|
4.2
|
19.2
|
1.0
|
HG23
|
C:ILE204
|
4.2
|
19.5
|
1.0
|
O
|
C:HOH998
|
4.2
|
34.3
|
1.0
|
O
|
C:HOH1043
|
4.3
|
45.0
|
1.0
|
N
|
C:ALA206
|
4.3
|
23.4
|
1.0
|
O
|
C:HOH1149
|
4.3
|
39.7
|
1.0
|
CB
|
C:MET207
|
4.4
|
18.9
|
1.0
|
N
|
C:VAL210
|
4.5
|
15.8
|
1.0
|
H
|
C:LEU212
|
4.5
|
17.7
|
1.0
|
C
|
C:ALA206
|
4.5
|
26.8
|
1.0
|
CA
|
C:VAL210
|
4.5
|
15.2
|
1.0
|
N
|
C:HIS211
|
4.5
|
14.9
|
1.0
|
CA
|
C:HIS211
|
4.6
|
16.5
|
1.0
|
CG2
|
C:ILE204
|
4.6
|
16.2
|
1.0
|
HD23
|
C:LEU205
|
4.6
|
38.7
|
1.0
|
HA
|
C:PRO208
|
4.7
|
23.7
|
1.0
|
N
|
C:PRO208
|
4.8
|
18.2
|
1.0
|
HB3
|
C:MET207
|
4.8
|
22.7
|
1.0
|
H
|
C:ALA206
|
4.8
|
28.1
|
1.0
|
CB
|
C:VAL210
|
4.9
|
15.9
|
1.0
|
CA
|
C:ALA206
|
4.9
|
30.2
|
1.0
|
CA
|
C:ILE204
|
4.9
|
17.4
|
1.0
|
HA
|
C:ILE204
|
5.0
|
20.9
|
1.0
|
H
|
C:LEU205
|
5.0
|
25.6
|
1.0
|
CB
|
C:LEU205
|
5.0
|
27.8
|
1.0
|
|
Reference:
R.S.Phillips,
K.N.Nguyen Hoang.
The Y430F Mutant of Salmonella D-Ornithine/D-Lysine Decarboxylase Has Altered Stereospecificity and A Putrescine Allosteric Activation Site. Arch.Biochem.Biophys. V. 731 09429 2022.
ISSN: ESSN 1096-0384
PubMed: 36265649
DOI: 10.1016/J.ABB.2022.109429
Page generated: Fri Apr 7 18:34:39 2023
|