Chlorine in PDB 6mpt: Tagt Bound to Li-Wta

Protein crystallography data

The structure of Tagt Bound to Li-Wta, PDB code: 6mpt was solved by T.W.Owens, K.Schaefer, D.Kahne, S.Walker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 59.87 / 1.65
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 66.231, 66.231, 140.036, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 22.2

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Tagt Bound to Li-Wta (pdb code 6mpt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Tagt Bound to Li-Wta, PDB code: 6mpt:

Chlorine binding site 1 out of 1 in 6mpt

Go back to Chlorine Binding Sites List in 6mpt
Chlorine binding site 1 out of 1 in the Tagt Bound to Li-Wta


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Tagt Bound to Li-Wta within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl402

b:28.1
occ:1.00
H A:LYS182 2.3 30.4 1.0
H A:SER183 2.8 33.7 1.0
O A:HOH644 2.9 32.9 1.0
HG13 A:VAL181 3.1 34.2 1.0
HA A:VAL181 3.1 29.7 1.0
N A:LYS182 3.2 25.2 1.0
HB3 A:SER183 3.2 38.8 1.0
O A:HOH716 3.4 34.0 1.0
HE1 A:TYR215 3.4 27.6 1.0
N A:SER183 3.5 28.0 1.0
HG21 A:VAL186 3.6 39.5 1.0
HG11 A:VAL186 3.6 34.7 1.0
HB A:VAL186 3.7 34.9 1.0
HB2 A:LYS182 3.8 31.5 1.0
OH A:TYR215 3.9 25.7 1.0
CA A:VAL181 3.9 24.7 1.0
CG1 A:VAL181 3.9 28.4 1.0
CB A:SER183 4.0 32.2 1.0
C A:VAL181 4.0 26.3 1.0
HG12 A:VAL181 4.1 34.2 1.0
CA A:LYS182 4.1 26.4 1.0
HB2 A:SER183 4.1 38.8 1.0
C A:LYS182 4.2 30.7 1.0
CE1 A:TYR215 4.2 22.9 1.0
CB A:VAL186 4.3 29.0 1.0
HG22 A:VAL181 4.3 35.9 1.0
CG2 A:VAL186 4.3 32.9 1.0
CG1 A:VAL186 4.3 28.9 1.0
CA A:SER183 4.3 29.0 1.0
HG3 A:LYS182 4.4 33.6 1.0
CB A:LYS182 4.4 26.2 1.0
CB A:VAL181 4.4 25.7 1.0
HH A:TYR215 4.6 31.0 1.0
CZ A:TYR215 4.6 25.6 1.0
HG23 A:VAL186 4.6 39.5 1.0
HG12 A:VAL186 4.6 34.7 1.0
HG11 A:VAL181 4.7 34.2 1.0
O A:THR180 4.7 25.2 1.0
O A:SER183 4.8 27.9 1.0
CG2 A:VAL181 4.9 29.8 1.0
CG A:LYS182 4.9 27.9 1.0
HA A:LYS182 5.0 31.8 1.0
HD3 A:ARG230 5.0 35.2 1.0

Reference:

K.Schaefer, T.W.Owens, D.Kahne, S.Walker. Substrate Preferences Establish the Order of Cell Wall Assembly in Staphylococcus Aureus. J. Am. Chem. Soc. V. 140 2442 2018.
ISSN: ESSN 1520-5126
PubMed: 29402087
DOI: 10.1021/JACS.7B13551
Page generated: Sat Dec 12 13:21:54 2020

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