Potassium in PDB 1u1d: Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau)
Enzymatic activity of Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau)
All present enzymatic activity of Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau):
2.4.2.3;
Protein crystallography data
The structure of Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau), PDB code: 1u1d
was solved by
W.Bu,
E.C.Settembre,
S.E.Ealick,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
47.14 /
2.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
91.150,
125.746,
140.880,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20.9 /
22.6
|
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau)
(pdb code 1u1d). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the
Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau), PDB code: 1u1d:
Jump to Potassium binding site number:
1;
2;
3;
Potassium binding site 1 out
of 3 in 1u1d
Go back to
Potassium Binding Sites List in 1u1d
Potassium binding site 1 out
of 3 in the Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau)
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 1 of Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:K1001
b:64.8
occ:1.00
|
O
|
A:ILE69
|
2.8
|
15.8
|
1.0
|
O
|
B:ILE69
|
2.8
|
15.8
|
1.0
|
OG
|
A:SER73
|
2.9
|
15.8
|
1.0
|
OG
|
B:SER73
|
2.9
|
15.8
|
1.0
|
OE1
|
B:GLU49
|
2.9
|
17.4
|
1.0
|
OE1
|
A:GLU49
|
3.0
|
16.4
|
1.0
|
O
|
A:HOH3451
|
3.1
|
47.1
|
1.0
|
CB
|
A:SER73
|
3.5
|
15.9
|
1.0
|
CB
|
B:SER73
|
3.5
|
16.1
|
1.0
|
N
|
B:ILE69
|
3.8
|
15.7
|
1.0
|
N
|
A:ILE69
|
3.8
|
16.1
|
1.0
|
C
|
B:ILE69
|
3.8
|
15.8
|
1.0
|
C
|
A:ILE69
|
3.9
|
15.9
|
1.0
|
CD
|
A:GLU49
|
4.1
|
17.0
|
1.0
|
CD
|
B:GLU49
|
4.1
|
17.5
|
1.0
|
C
|
B:GLY68
|
4.3
|
15.7
|
1.0
|
C
|
A:GLY68
|
4.3
|
16.2
|
1.0
|
CA
|
B:ILE69
|
4.3
|
15.8
|
1.0
|
CA
|
A:ILE69
|
4.4
|
15.9
|
1.0
|
CA
|
A:GLY68
|
4.4
|
16.3
|
1.0
|
CA
|
B:GLY68
|
4.4
|
15.7
|
1.0
|
CG
|
A:GLU49
|
4.5
|
16.8
|
1.0
|
CG
|
B:GLU49
|
4.5
|
17.0
|
1.0
|
CB
|
B:ILE69
|
4.7
|
15.8
|
1.0
|
CA
|
A:SER73
|
4.8
|
16.0
|
1.0
|
CA
|
B:SER73
|
4.8
|
16.1
|
1.0
|
N
|
A:SER73
|
4.8
|
16.0
|
1.0
|
O
|
A:THR67
|
4.9
|
16.4
|
1.0
|
N
|
B:SER73
|
4.9
|
16.1
|
1.0
|
CB
|
A:ILE69
|
4.9
|
15.9
|
1.0
|
O
|
B:THR67
|
4.9
|
15.6
|
1.0
|
N
|
B:GLY70
|
5.0
|
15.8
|
1.0
|
N
|
A:GLY70
|
5.0
|
15.9
|
1.0
|
|
Potassium binding site 2 out
of 3 in 1u1d
Go back to
Potassium Binding Sites List in 1u1d
Potassium binding site 2 out
of 3 in the Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau)
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 2 of Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:K1002
b:56.2
occ:1.00
|
OG
|
D:SER73
|
2.8
|
13.8
|
1.0
|
O
|
D:ILE69
|
2.8
|
14.5
|
1.0
|
O
|
C:ILE69
|
2.9
|
15.1
|
1.0
|
OE1
|
D:GLU49
|
2.9
|
16.4
|
1.0
|
OG
|
C:SER73
|
2.9
|
14.3
|
1.0
|
OE1
|
C:GLU49
|
3.0
|
17.3
|
1.0
|
O
|
D:HOH6444
|
3.2
|
37.7
|
1.0
|
CB
|
D:SER73
|
3.5
|
14.4
|
1.0
|
CB
|
C:SER73
|
3.6
|
14.5
|
1.0
|
N
|
C:ILE69
|
3.7
|
15.2
|
1.0
|
N
|
D:ILE69
|
3.8
|
14.6
|
1.0
|
C
|
D:ILE69
|
3.9
|
14.6
|
1.0
|
C
|
C:ILE69
|
3.9
|
15.2
|
1.0
|
CD
|
D:GLU49
|
4.0
|
16.2
|
1.0
|
CD
|
C:GLU49
|
4.0
|
16.9
|
1.0
|
C
|
C:GLY68
|
4.3
|
15.1
|
1.0
|
C
|
D:GLY68
|
4.3
|
14.7
|
1.0
|
CA
|
C:ILE69
|
4.3
|
15.0
|
1.0
|
CA
|
D:ILE69
|
4.3
|
14.6
|
1.0
|
CA
|
C:GLY68
|
4.4
|
15.2
|
1.0
|
CA
|
D:GLY68
|
4.4
|
14.8
|
1.0
|
CG
|
C:GLU49
|
4.4
|
16.2
|
1.0
|
CG
|
D:GLU49
|
4.4
|
15.8
|
1.0
|
CA
|
D:SER73
|
4.8
|
14.3
|
1.0
|
CB
|
C:ILE69
|
4.8
|
15.2
|
1.0
|
O
|
D:THR67
|
4.8
|
15.1
|
1.0
|
O
|
C:THR67
|
4.8
|
15.3
|
1.0
|
CB
|
D:ILE69
|
4.8
|
14.7
|
1.0
|
N
|
D:SER73
|
4.8
|
14.3
|
1.0
|
CA
|
C:SER73
|
4.9
|
14.4
|
1.0
|
N
|
C:SER73
|
4.9
|
14.5
|
1.0
|
N
|
D:GLY70
|
5.0
|
14.6
|
1.0
|
|
Potassium binding site 3 out
of 3 in 1u1d
Go back to
Potassium Binding Sites List in 1u1d
Potassium binding site 3 out
of 3 in the Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau)
 Mono view
 Stereo pair view
|
A full contact list of Potassium with other atoms in the K binding
site number 3 of Structure of E. Coli Uridine Phosphorylase Complexed to 5- (Phenylthio)Acyclouridine (Ptau) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:K1003
b:74.2
occ:1.00
|
OG
|
F:SER73
|
2.8
|
15.2
|
1.0
|
O
|
E:ILE69
|
2.9
|
14.9
|
1.0
|
O
|
F:ILE69
|
2.9
|
15.7
|
1.0
|
OG
|
E:SER73
|
3.0
|
15.1
|
1.0
|
OE1
|
F:GLU49
|
3.0
|
16.4
|
1.0
|
OE1
|
E:GLU49
|
3.1
|
16.5
|
1.0
|
CB
|
F:SER73
|
3.7
|
15.5
|
1.0
|
CB
|
E:SER73
|
3.8
|
15.4
|
1.0
|
N
|
F:ILE69
|
3.9
|
15.8
|
1.0
|
N
|
E:ILE69
|
3.9
|
15.1
|
1.0
|
C
|
E:ILE69
|
3.9
|
15.0
|
1.0
|
C
|
F:ILE69
|
4.0
|
15.7
|
1.0
|
CD
|
F:GLU49
|
4.1
|
16.4
|
1.0
|
CD
|
E:GLU49
|
4.2
|
16.8
|
1.0
|
CA
|
E:ILE69
|
4.4
|
15.0
|
1.0
|
CA
|
F:ILE69
|
4.4
|
15.7
|
1.0
|
C
|
F:GLY68
|
4.4
|
15.8
|
1.0
|
C
|
E:GLY68
|
4.4
|
15.3
|
1.0
|
CA
|
F:GLY68
|
4.5
|
15.8
|
1.0
|
CA
|
E:GLY68
|
4.6
|
15.4
|
1.0
|
CG
|
E:GLU49
|
4.6
|
16.8
|
1.0
|
CG
|
F:GLU49
|
4.6
|
16.3
|
1.0
|
CB
|
E:ILE69
|
4.8
|
15.0
|
1.0
|
CB
|
F:ILE69
|
4.9
|
15.7
|
1.0
|
N
|
F:SER73
|
4.9
|
15.5
|
1.0
|
O
|
F:THR67
|
4.9
|
15.9
|
1.0
|
CA
|
F:SER73
|
4.9
|
15.5
|
1.0
|
N
|
E:SER73
|
4.9
|
15.4
|
1.0
|
CA
|
E:SER73
|
5.0
|
15.4
|
1.0
|
|
Reference:
W.Bu,
E.C.Settembre,
M.H.El Kouni,
S.E.Ealick.
Structural Basis For Inhibition of Escherichia Coli Uridine Phosphorylase By 5-Substituted Acyclouridines. Acta Crystallogr.,Sect.D V. 61 863 2005.
ISSN: ISSN 0907-4449
PubMed: 15983408
DOI: 10.1107/S0907444905007882
Page generated: Mon Aug 12 05:32:35 2024
|