Chlorine in PDB 7c4g: A Legionella Acetyltransferase Vipf

Protein crystallography data

The structure of A Legionella Acetyltransferase Vipf, PDB code: 7c4g was solved by T.T.Chen, Y.L.Lin, Z.Chen, A.D.Han, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.24 / 2.30
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 72.042, 84.528, 105.544, 90, 90, 90
R / Rfree (%) 23.8 / 29.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the A Legionella Acetyltransferase Vipf (pdb code 7c4g). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the A Legionella Acetyltransferase Vipf, PDB code: 7c4g:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 7c4g

Go back to Chlorine Binding Sites List in 7c4g
Chlorine binding site 1 out of 2 in the A Legionella Acetyltransferase Vipf


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of A Legionella Acetyltransferase Vipf within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:117.8
occ:1.00
CL1 A:CLM303 0.0 117.8 1.0
C1 A:CLM303 1.8 106.4 1.0
H1 A:CLM303 2.2 127.8 1.0
C2 A:CLM303 2.9 96.2 1.0
O2 A:CLM303 3.0 103.3 1.0
CL2 A:CLM303 3.0 108.0 1.0
OE1 A:GLU129 3.4 52.6 1.0
OE1 A:GLU253 3.7 48.7 1.0
CD A:GLU253 3.8 49.8 1.0
CD A:GLU129 3.8 53.4 1.0
OE2 A:GLU129 3.8 62.9 1.0
OH A:TYR276 3.9 48.6 1.0
OE2 A:GLU253 3.9 47.1 1.0
N2 A:CLM303 4.2 84.8 1.0
HN2 A:CLM303 4.4 101.8 1.0
CG A:GLU253 4.6 47.6 1.0
CZ A:TYR276 4.6 45.2 1.0
CE1 A:TYR276 4.9 38.2 1.0
CG A:GLU129 5.0 34.9 1.0
HO5 A:CLM303 5.0 95.1 1.0

Chlorine binding site 2 out of 2 in 7c4g

Go back to Chlorine Binding Sites List in 7c4g
Chlorine binding site 2 out of 2 in the A Legionella Acetyltransferase Vipf


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of A Legionella Acetyltransferase Vipf within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl303

b:108.0
occ:1.00
CL2 A:CLM303 0.0 108.0 1.0
C1 A:CLM303 1.8 106.4 1.0
H1 A:CLM303 2.2 127.8 1.0
HN2 A:CLM303 2.8 101.8 1.0
C2 A:CLM303 2.8 96.2 1.0
CL1 A:CLM303 3.0 117.8 1.0
N2 A:CLM303 3.2 84.8 1.0
O2 A:CLM303 3.8 103.3 1.0
OE2 A:GLU129 4.0 62.9 1.0
OE1 A:GLU253 4.1 48.7 1.0
O4 A:CLM303 4.4 87.9 1.0
C3 A:CLM303 4.5 83.0 1.0
H3 A:CLM303 4.8 99.7 1.0
HO4 A:CLM303 4.8 105.5 1.0
CD A:GLU129 4.8 53.4 1.0
CD A:GLU253 4.9 49.8 1.0

Reference:

T.T.Chen, Y.L.Lin, Z.Chen, A.D.Han. Structural Basis For Acetyltransferase Mechanism of A Legionella Effector Vipf To Be Published.
Page generated: Sat Jul 10 12:36:03 2021

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