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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: Sun Dec 13 23:02:25 2020

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