Sodium in PDB 8d5d: Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with D- Arginine
Enzymatic activity of Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with D- Arginine
All present enzymatic activity of Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with D- Arginine:
4.1.1.116;
Protein crystallography data
The structure of Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with D- Arginine, PDB code: 8d5d
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)
|
48.86 /
1.54
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
141.77,
49.54,
139.56,
90,
115.93,
90
|
R / Rfree (%)
|
16.1 /
19.3
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with D- Arginine
(pdb code 8d5d). 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 D- Arginine, PDB code: 8d5d:
Jump to Sodium binding site number:
1;
2;
Sodium binding site 1 out
of 2 in 8d5d
Go back to
Sodium Binding Sites List in 8d5d
Sodium binding site 1 out
of 2 in the Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with D- Arginine
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 D- Arginine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na507
b:29.1
occ:1.00
|
O
|
A:VAL210
|
2.4
|
30.9
|
1.0
|
O
|
A:ILE204
|
2.4
|
31.8
|
1.0
|
O
|
A:MET207
|
2.4
|
37.4
|
1.0
|
O
|
A:LEU205
|
2.8
|
38.8
|
1.0
|
HA
|
A:LEU205
|
3.0
|
42.4
|
1.0
|
C
|
A:LEU205
|
3.3
|
37.6
|
1.0
|
H
|
A:MET207
|
3.4
|
39.9
|
1.0
|
C
|
A:ILE204
|
3.5
|
28.4
|
1.0
|
C
|
A:MET207
|
3.5
|
36.5
|
1.0
|
O
|
A:HOH864
|
3.6
|
39.6
|
1.0
|
CA
|
A:LEU205
|
3.6
|
35.3
|
1.0
|
C
|
A:VAL210
|
3.6
|
26.2
|
1.0
|
HB2
|
A:MET207
|
3.6
|
36.0
|
1.0
|
H
|
A:VAL210
|
3.6
|
35.0
|
1.0
|
N
|
A:MET207
|
3.7
|
33.3
|
1.0
|
HA
|
A:HIS211
|
3.9
|
29.6
|
1.0
|
HG22
|
A:ILE204
|
4.0
|
35.0
|
1.0
|
N
|
A:LEU205
|
4.0
|
32.1
|
1.0
|
CA
|
A:MET207
|
4.0
|
31.7
|
1.0
|
O
|
A:HOH883
|
4.0
|
54.2
|
1.0
|
HB
|
A:VAL210
|
4.1
|
28.8
|
1.0
|
HG23
|
A:ILE204
|
4.1
|
35.0
|
1.0
|
N
|
A:ALA206
|
4.2
|
33.0
|
1.0
|
O
|
A:HOH902
|
4.2
|
46.0
|
1.0
|
CB
|
A:MET207
|
4.3
|
30.0
|
1.0
|
N
|
A:VAL210
|
4.3
|
29.2
|
1.0
|
C
|
A:ALA206
|
4.4
|
39.6
|
1.0
|
CA
|
A:VAL210
|
4.5
|
25.5
|
1.0
|
CG2
|
A:ILE204
|
4.5
|
29.1
|
1.0
|
N
|
A:HIS211
|
4.6
|
27.3
|
1.0
|
HA
|
A:PRO208
|
4.6
|
42.7
|
1.0
|
H
|
A:LEU212
|
4.6
|
32.8
|
1.0
|
N
|
A:PRO208
|
4.6
|
34.6
|
1.0
|
CA
|
A:HIS211
|
4.7
|
24.6
|
1.0
|
HB3
|
A:MET207
|
4.7
|
36.0
|
1.0
|
HD22
|
A:LEU205
|
4.7
|
45.6
|
1.0
|
H
|
A:ALA206
|
4.7
|
39.6
|
1.0
|
CA
|
A:ILE204
|
4.7
|
29.2
|
1.0
|
HA
|
A:ILE204
|
4.7
|
35.0
|
1.0
|
CA
|
A:ALA206
|
4.8
|
40.1
|
1.0
|
CB
|
A:VAL210
|
4.8
|
24.0
|
1.0
|
C
|
A:PRO208
|
4.8
|
36.2
|
1.0
|
H
|
A:LEU205
|
4.8
|
38.6
|
1.0
|
O
|
A:PRO208
|
4.9
|
35.4
|
1.0
|
CA
|
A:PRO208
|
4.9
|
35.6
|
1.0
|
HA
|
A:ALA206
|
4.9
|
48.1
|
1.0
|
CB
|
A:LEU205
|
4.9
|
38.4
|
1.0
|
HA
|
A:MET207
|
5.0
|
38.0
|
1.0
|
|
Sodium binding site 2 out
of 2 in 8d5d
Go back to
Sodium Binding Sites List in 8d5d
Sodium binding site 2 out
of 2 in the Structure of Y430F D-Ornithine/D-Lysine Decarboxylase Complex with D- Arginine
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 D- Arginine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Na506
b:31.6
occ:1.00
|
O
|
B:HOH933
|
2.0
|
40.3
|
1.0
|
O
|
B:VAL210
|
2.3
|
32.1
|
1.0
|
O
|
B:MET207
|
2.4
|
39.6
|
1.0
|
O
|
B:ILE204
|
2.6
|
34.0
|
1.0
|
O
|
B:LEU205
|
2.9
|
43.7
|
1.0
|
HA
|
B:LEU205
|
3.2
|
42.0
|
1.0
|
C
|
B:LEU205
|
3.3
|
44.0
|
1.0
|
C
|
B:MET207
|
3.5
|
36.9
|
1.0
|
H
|
B:MET207
|
3.6
|
40.3
|
1.0
|
C
|
B:VAL210
|
3.6
|
29.5
|
1.0
|
H
|
B:VAL210
|
3.6
|
36.9
|
1.0
|
HB2
|
B:MET207
|
3.7
|
44.1
|
1.0
|
C
|
B:ILE204
|
3.7
|
35.5
|
1.0
|
CA
|
B:LEU205
|
3.7
|
35.0
|
1.0
|
O
|
B:HOH959
|
3.7
|
49.5
|
1.0
|
N
|
B:MET207
|
3.8
|
33.5
|
1.0
|
HA
|
B:HIS211
|
3.9
|
35.9
|
1.0
|
HB
|
B:VAL210
|
4.0
|
37.6
|
1.0
|
CA
|
B:MET207
|
4.1
|
35.0
|
1.0
|
HG21
|
B:ILE204
|
4.2
|
38.9
|
1.0
|
N
|
B:LEU205
|
4.2
|
34.2
|
1.0
|
O
|
B:HOH846
|
4.2
|
51.0
|
1.0
|
O
|
B:HOH881
|
4.2
|
38.5
|
1.0
|
N
|
B:ALA206
|
4.2
|
37.6
|
1.0
|
HG22
|
B:ILE204
|
4.3
|
38.9
|
1.0
|
N
|
B:VAL210
|
4.3
|
30.7
|
1.0
|
CB
|
B:MET207
|
4.3
|
36.7
|
1.0
|
C
|
B:ALA206
|
4.4
|
34.8
|
1.0
|
CA
|
B:VAL210
|
4.4
|
27.2
|
1.0
|
N
|
B:HIS211
|
4.5
|
30.2
|
1.0
|
HA
|
B:PRO208
|
4.6
|
38.1
|
1.0
|
N
|
B:PRO208
|
4.7
|
37.9
|
1.0
|
CA
|
B:HIS211
|
4.7
|
29.9
|
1.0
|
CG2
|
B:ILE204
|
4.7
|
32.4
|
1.0
|
CB
|
B:VAL210
|
4.7
|
31.4
|
1.0
|
HD21
|
B:LEU205
|
4.7
|
57.8
|
1.0
|
H
|
B:LEU212
|
4.7
|
37.0
|
1.0
|
CA
|
B:ALA206
|
4.8
|
39.7
|
1.0
|
H
|
B:ALA206
|
4.8
|
45.1
|
1.0
|
HB3
|
B:MET207
|
4.8
|
44.1
|
1.0
|
C
|
B:PRO208
|
4.9
|
35.0
|
1.0
|
HA
|
B:ALA206
|
4.9
|
47.6
|
1.0
|
CA
|
B:PRO208
|
4.9
|
31.8
|
1.0
|
CA
|
B:ILE204
|
4.9
|
39.7
|
1.0
|
HA
|
B:ILE204
|
4.9
|
47.6
|
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: Wed Oct 9 11:22:26 2024
|