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Chlorine in PDB 4da5: Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology

Enzymatic activity of Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology

All present enzymatic activity of Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology:
2.7.1.32; 2.7.1.82;

Protein crystallography data

The structure of Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology, PDB code: 4da5 was solved by K.Brown, C.Hudson, P.Charlton, J.Pollard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.50 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.840, 121.690, 131.730, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 25.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology (pdb code 4da5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology, PDB code: 4da5:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 4da5

Go back to Chlorine Binding Sites List in 4da5
Chlorine binding site 1 out of 4 in the Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:68.4
occ:1.00
 CL1 A:0H7502 0.0 68.4 1.0
C14 A:0H7502 1.7 54.9 1.0
OH A:TYR437 2.7 31.6 1.0
C13 A:0H7502 2.7 50.7 1.0
S16 A:0H7502 3.1 47.9 1.0
CZ A:TYR437 3.4 32.5 1.0
CE1 A:TYR437 3.6 26.2 1.0
CB A:PHE435 3.9 25.5 1.0
CG2 A:ILE433 3.9 38.3 1.0
C12 A:0H7502 3.9 50.1 1.0
CG A:PHE435 4.0 25.4 1.0
O A:HOH698 4.2 44.5 1.0
C11 A:0H7502 4.2 49.3 1.0
CB A:ILE433 4.3 37.7 1.0
CD1 A:PHE435 4.3 26.4 1.0
CD1 A:ILE433 4.5 48.9 1.0
CD2 A:PHE435 4.5 24.9 1.0
CE2 A:TYR437 4.6 27.0 1.0
CH2 A:TRP423 4.6 28.4 1.0
CD1 A:TYR437 4.8 26.4 1.0
O A:HOH669 4.9 50.6 1.0

Chlorine binding site 2 out of 4 in 4da5

Go back to Chlorine Binding Sites List in 4da5
Chlorine binding site 2 out of 4 in the Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:83.7
occ:1.00
 CL2 A:0H7502 0.0 83.7 1.0
C20 A:0H7502 1.7 75.2 1.0
C19 A:0H7502 2.8 68.9 1.0
S22 A:0H7502 3.1 72.0 1.0
OE1 A:GLN308 3.5 47.7 1.0
CA A:GLY310 3.8 30.6 1.0
CB A:TYR354 3.9 29.7 1.0
C18 A:0H7502 4.0 65.0 1.0
NE2 A:GLN308 4.0 52.2 1.0
CD A:GLN308 4.2 57.0 1.0
CD2 A:TYR354 4.2 32.6 1.0
C17 A:0H7502 4.2 63.7 1.0
N A:GLY310 4.3 31.6 1.0
CG A:TYR354 4.4 31.4 1.0
O A:HOH616 4.5 38.7 1.0
O A:HOH636 4.8 38.8 1.0
C A:GLY310 5.0 32.5 1.0

Chlorine binding site 3 out of 4 in 4da5

Go back to Chlorine Binding Sites List in 4da5
Chlorine binding site 3 out of 4 in the Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:89.3
occ:1.00
 CL1 B:0H7502 0.0 89.3 1.0
C14 B:0H7502 1.7 82.7 1.0
OH B:TYR437 2.7 50.9 1.0
C13 B:0H7502 2.7 80.1 1.0
S16 B:0H7502 3.1 78.9 1.0
CZ B:TYR437 3.3 47.4 1.0
CB B:PHE435 3.4 35.6 1.0
CG B:PHE435 3.5 35.9 1.0
CE1 B:TYR437 3.6 40.4 1.0
CG2 B:ILE433 3.6 54.3 1.0
CD2 B:PHE435 3.8 37.3 1.0
C12 B:0H7502 3.9 78.9 1.0
CD1 B:PHE435 4.1 39.0 1.0
C11 B:0H7502 4.2 78.6 1.0
CE2 B:TYR437 4.2 39.5 1.0
CB B:ILE433 4.2 54.1 1.0
O B:HOH685 4.3 37.5 1.0
CE2 B:PHE435 4.6 39.4 1.0
CD1 B:TYR437 4.7 37.8 1.0
CD1 B:ILE433 4.8 61.5 1.0
CE1 B:PHE435 4.8 39.1 1.0
CA B:PHE435 4.9 35.6 1.0

Chlorine binding site 4 out of 4 in 4da5

Go back to Chlorine Binding Sites List in 4da5
Chlorine binding site 4 out of 4 in the Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Choline Kinase Alpha Acts Through A Double-Displacement Kinetic Mechanism Involving Enzyme Isomerisation, As Determined Through Enzyme and Inhibitor Kinetics and Structural Biology within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl502

b:95.2
occ:1.00
 CL2 B:0H7502 0.0 95.2 1.0
C20 B:0H7502 1.7 91.2 1.0
C19 B:0H7502 2.7 88.9 1.0
S22 B:0H7502 3.1 88.8 1.0
O B:HOH662 3.1 33.3 1.0
C18 B:0H7502 4.0 87.1 1.0
CA B:GLY310 4.0 26.5 1.0
OE1 B:GLN308 4.1 48.0 1.0
NE2 B:GLN308 4.2 48.4 1.0
C17 B:0H7502 4.2 84.8 1.0
CB B:TYR354 4.5 27.0 1.0
O B:HOH685 4.5 37.5 1.0
CD B:GLN308 4.6 55.1 1.0
CD2 B:TYR354 4.7 27.7 1.0
N B:GLY310 4.8 28.4 1.0
O B:HOH661 4.8 37.2 1.0
CG B:TYR354 5.0 27.9 1.0

Reference:

C.S.Hudson, R.M.Knegtel, K.Brown, P.A.Charlton, J.R.Pollard. Kinetic and Mechanistic Characterisation of Choline Kinase-Alpha. Biochim.Biophys.Acta V.1834 1107 2013.
ISSN: ISSN 0006-3002
PubMed: 23416529
DOI: 10.1016/J.BBAPAP.2013.02.008
Page generated: Sun Jul 21 11:52:40 2024

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