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Chlorine in PDB 5tui: Crystal Structure of Tetracycline Destructase Tet(50) in Complex with Chlortetracycline

Protein crystallography data

The structure of Crystal Structure of Tetracycline Destructase Tet(50) in Complex with Chlortetracycline, PDB code: 5tui was solved by J.Park, N.H.Tolia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.77 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.100, 107.220, 152.630, 90.00, 90.00, 90.00
R / Rfree (%) 17.8 / 21.9

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Tetracycline Destructase Tet(50) in Complex with Chlortetracycline (pdb code 5tui). 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 Crystal Structure of Tetracycline Destructase Tet(50) in Complex with Chlortetracycline, PDB code: 5tui:

Chlorine binding site 1 out of 1 in 5tui

Go back to Chlorine Binding Sites List in 5tui
Chlorine binding site 1 out of 1 in the Crystal Structure of Tetracycline Destructase Tet(50) in Complex with Chlortetracycline


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Tetracycline Destructase Tet(50) in Complex with Chlortetracycline within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl405

b:52.4
occ:1.00
CL7 B:CTC405 0.0 52.4 1.0
C7 B:CTC405 1.8 44.6 1.0
H6'1 B:CTC405 2.3 47.9 1.0
C8 B:CTC405 2.6 28.2 1.0
H6 B:FAD404 2.6 26.5 1.0
H8 B:CTC405 2.7 33.8 1.0
HM72 B:FAD404 2.8 32.1 1.0
C6A B:CTC405 2.9 36.0 1.0
C6' B:CTC405 3.1 40.0 1.0
HO6 B:CTC405 3.2 46.2 1.0
H6'2 B:CTC405 3.4 47.9 1.0
C6 B:CTC405 3.4 35.8 1.0
HG21 B:VAL181 3.6 27.3 1.0
C7M B:FAD404 3.6 26.8 1.0
C6 B:FAD404 3.7 22.1 1.0
HM71 B:FAD404 3.7 32.1 1.0
O B:HOH679 3.7 28.2 1.0
O6 B:CTC405 3.8 38.5 1.0
O B:HOH594 3.9 30.4 1.0
HG22 B:VAL181 3.9 27.3 1.0
C9 B:CTC405 4.0 38.7 1.0
H6'3 B:CTC405 4.0 47.9 1.0
HE3 B:MET222 4.0 41.0 1.0
CG2 B:VAL181 4.1 22.8 1.0
HG23 B:VAL181 4.1 27.3 1.0
C7 B:FAD404 4.2 22.9 1.0
HB2 B:ALA183 4.2 23.0 1.0
C6B B:CTC405 4.2 38.5 1.0
HM73 B:FAD404 4.5 32.1 1.0
C10 B:CTC405 4.6 42.1 1.0
HB3 B:PRO296 4.6 25.1 1.0
HA3 B:GLY220 4.7 18.6 1.0
H9 B:CTC405 4.8 46.4 1.0
C5X B:FAD404 4.8 23.0 1.0
C5A B:CTC405 4.9 30.1 1.0
CE B:MET222 4.9 34.1 1.0
HB2 B:GLN44 4.9 24.9 1.0
H5A B:CTC405 4.9 36.1 1.0
N5 B:FAD404 5.0 24.8 1.0
HE2 B:MET222 5.0 41.0 1.0

Reference:

J.Park, A.J.Gasparrini, M.R.Reck, C.T.Symister, J.L.Elliott, J.P.Vogel, T.A.Wencewicz, G.Dantas, N.H.Tolia. Plasticity, Dynamics, and Inhibition of Emerging Tetracycline Resistance Enzymes. Nat. Chem. Biol. V. 13 730 2017.
ISSN: ESSN 1552-4469
PubMed: 28481346
DOI: 10.1038/NCHEMBIO.2376
Page generated: Sat Jul 12 09:07:23 2025

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