Potassium in PDB 5uam: Structure of A New Family of Polysaccharide Lyase PL25-Ulvanlyase.
Protein crystallography data
The structure of Structure of A New Family of Polysaccharide Lyase PL25-Ulvanlyase., PDB code: 5uam
was solved by
T.S.Ulaganathan,
M.T.Boniecki,
M.Cygler,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
45.20 /
1.45
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
174.260,
72.110,
109.510,
90.00,
122.50,
90.00
|
R / Rfree (%)
|
13.4 /
14.3
|
Other elements in 5uam:
The structure of Structure of A New Family of Polysaccharide Lyase PL25-Ulvanlyase. also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of A New Family of Polysaccharide Lyase PL25-Ulvanlyase.
(pdb code 5uam). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the
Structure of A New Family of Polysaccharide Lyase PL25-Ulvanlyase., PDB code: 5uam:
Jump to Potassium binding site number:
1;
2;
Potassium binding site 1 out
of 2 in 5uam
Go back to
Potassium Binding Sites List in 5uam
Potassium binding site 1 out
of 2 in the Structure of A New Family of Polysaccharide Lyase PL25-Ulvanlyase.
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structure of A New Family of Polysaccharide Lyase PL25-Ulvanlyase. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K505
b:17.3
occ:1.00
|
H
|
A:ILE64
|
2.6
|
13.7
|
1.0
|
HB
|
A:ILE64
|
3.1
|
14.7
|
1.0
|
O
|
A:HOH1018
|
3.1
|
13.5
|
1.0
|
O
|
A:HOH1021
|
3.2
|
16.4
|
1.0
|
O
|
A:HOH969
|
3.2
|
14.8
|
1.0
|
O
|
A:HOH930
|
3.2
|
17.3
|
1.0
|
HE2
|
A:PHE329
|
3.3
|
18.5
|
1.0
|
HD12
|
A:ILE64
|
3.4
|
19.1
|
1.0
|
N
|
A:ILE64
|
3.4
|
11.4
|
1.0
|
HB1
|
A:ALA63
|
3.4
|
14.4
|
1.0
|
HA
|
A:ALA63
|
3.5
|
13.4
|
1.0
|
HD2
|
A:ARG386
|
3.5
|
15.6
|
1.0
|
HG13
|
A:ILE64
|
3.7
|
17.2
|
1.0
|
HG3
|
A:ARG386
|
3.8
|
18.1
|
1.0
|
CB
|
A:ILE64
|
3.9
|
12.2
|
1.0
|
HB3
|
A:ARG386
|
4.0
|
16.1
|
1.0
|
HE
|
A:ARG386
|
4.1
|
17.4
|
1.0
|
CG1
|
A:ILE64
|
4.1
|
14.3
|
1.0
|
O
|
A:HOH721
|
4.1
|
14.7
|
1.0
|
CA
|
A:ALA63
|
4.1
|
11.2
|
1.0
|
CB
|
A:ALA63
|
4.1
|
12.0
|
1.0
|
CD1
|
A:ILE64
|
4.2
|
15.9
|
1.0
|
CE2
|
A:PHE329
|
4.2
|
15.4
|
1.0
|
CD
|
A:ARG386
|
4.3
|
13.0
|
1.0
|
C
|
A:ALA63
|
4.3
|
12.3
|
1.0
|
CA
|
A:ILE64
|
4.3
|
11.8
|
1.0
|
O
|
A:HOH1097
|
4.3
|
16.9
|
1.0
|
CG
|
A:ARG386
|
4.4
|
15.0
|
1.0
|
H
|
A:VAL65
|
4.4
|
13.0
|
1.0
|
HB2
|
A:ALA63
|
4.4
|
14.4
|
1.0
|
HZ
|
A:PHE329
|
4.5
|
18.2
|
1.0
|
NE
|
A:ARG386
|
4.6
|
14.5
|
1.0
|
HG13
|
A:ILE439
|
4.6
|
15.6
|
1.0
|
CB
|
A:ARG386
|
4.6
|
13.4
|
1.0
|
O
|
A:ILE439
|
4.7
|
14.7
|
1.0
|
HD11
|
A:ILE64
|
4.7
|
19.1
|
1.0
|
HD13
|
A:ILE64
|
4.8
|
19.1
|
1.0
|
CZ
|
A:PHE329
|
4.8
|
15.1
|
1.0
|
O
|
A:HOH1143
|
4.9
|
15.3
|
1.0
|
H
|
A:ILE439
|
4.9
|
15.5
|
1.0
|
HB2
|
A:ARG386
|
4.9
|
16.1
|
1.0
|
O
|
A:HOH742
|
4.9
|
21.3
|
1.0
|
O
|
A:HOH1129
|
4.9
|
25.0
|
1.0
|
HB3
|
A:ALA63
|
5.0
|
14.4
|
1.0
|
HA
|
A:ILE64
|
5.0
|
14.2
|
1.0
|
|
Potassium binding site 2 out
of 2 in 5uam
Go back to
Potassium Binding Sites List in 5uam
Potassium binding site 2 out
of 2 in the Structure of A New Family of Polysaccharide Lyase PL25-Ulvanlyase.
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structure of A New Family of Polysaccharide Lyase PL25-Ulvanlyase. within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:K504
b:17.6
occ:1.00
|
H
|
B:ILE64
|
2.5
|
14.4
|
1.0
|
HB
|
B:ILE64
|
3.0
|
16.0
|
1.0
|
O
|
B:HOH1003
|
3.1
|
14.3
|
1.0
|
O
|
B:HOH935
|
3.2
|
18.3
|
1.0
|
O
|
B:HOH983
|
3.2
|
17.0
|
1.0
|
O
|
B:HOH942
|
3.2
|
15.1
|
1.0
|
HE2
|
B:PHE329
|
3.3
|
18.6
|
1.0
|
HD12
|
B:ILE64
|
3.3
|
20.9
|
1.0
|
N
|
B:ILE64
|
3.4
|
12.0
|
1.0
|
HB1
|
B:ALA63
|
3.5
|
15.0
|
1.0
|
HD2
|
B:ARG386
|
3.5
|
18.6
|
1.0
|
HA
|
B:ALA63
|
3.6
|
14.4
|
1.0
|
HG13
|
B:ILE64
|
3.7
|
16.7
|
1.0
|
HG3
|
B:ARG386
|
3.7
|
18.9
|
1.0
|
CB
|
B:ILE64
|
3.8
|
13.3
|
1.0
|
HB3
|
B:ARG386
|
4.0
|
18.6
|
1.0
|
CG1
|
B:ILE64
|
4.0
|
13.9
|
1.0
|
HE
|
B:ARG386
|
4.0
|
19.3
|
1.0
|
CD1
|
B:ILE64
|
4.1
|
17.4
|
1.0
|
O
|
B:HOH716
|
4.1
|
15.1
|
1.0
|
CE2
|
B:PHE329
|
4.2
|
15.4
|
1.0
|
CA
|
B:ALA63
|
4.2
|
11.9
|
1.0
|
CD
|
B:ARG386
|
4.2
|
15.5
|
1.0
|
CB
|
B:ALA63
|
4.2
|
12.4
|
1.0
|
CA
|
B:ILE64
|
4.2
|
12.5
|
1.0
|
CG
|
B:ARG386
|
4.3
|
15.8
|
1.0
|
C
|
B:ALA63
|
4.3
|
12.3
|
1.0
|
O
|
B:HOH1071
|
4.4
|
17.3
|
1.0
|
H
|
B:VAL65
|
4.4
|
14.3
|
1.0
|
HZ
|
B:PHE329
|
4.5
|
19.2
|
1.0
|
HB2
|
B:ALA63
|
4.5
|
15.0
|
1.0
|
NE
|
B:ARG386
|
4.5
|
16.1
|
1.0
|
HG13
|
B:ILE439
|
4.6
|
16.6
|
1.0
|
HD11
|
B:ILE64
|
4.6
|
20.9
|
1.0
|
CB
|
B:ARG386
|
4.6
|
15.5
|
1.0
|
O
|
B:ILE439
|
4.6
|
13.5
|
1.0
|
HD13
|
B:ILE64
|
4.7
|
20.9
|
1.0
|
CZ
|
B:PHE329
|
4.8
|
16.0
|
1.0
|
O
|
B:HOH1128
|
4.8
|
15.8
|
1.0
|
HB2
|
B:ARG386
|
4.9
|
18.6
|
1.0
|
H
|
B:ILE439
|
4.9
|
14.8
|
1.0
|
O
|
B:HOH797
|
4.9
|
18.9
|
1.0
|
HA
|
B:ILE64
|
4.9
|
15.0
|
1.0
|
HG12
|
B:ILE64
|
5.0
|
16.7
|
1.0
|
|
Reference:
T.Ulaganathan,
M.T.Boniecki,
E.Foran,
V.Buravenkov,
N.Mizrachi,
E.Banin,
W.Helbert,
M.Cygler.
New Ulvan-Degrading Polysaccharide Lyase Family: Structure and Catalytic Mechanism Suggests Convergent Evolution of Active Site Architecture. Acs Chem. Biol. V. 12 1269 2017.
ISSN: ESSN 1554-8937
PubMed: 28290654
DOI: 10.1021/ACSCHEMBIO.7B00126
Page generated: Mon Aug 12 14:40:49 2024
|