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Chlorine in PDB 4leq: Trna Guanine Transglycosylase (Tgt) in Complex with Furanoside-Based Lin-Benzoguanine 1

Enzymatic activity of Trna Guanine Transglycosylase (Tgt) in Complex with Furanoside-Based Lin-Benzoguanine 1

All present enzymatic activity of Trna Guanine Transglycosylase (Tgt) in Complex with Furanoside-Based Lin-Benzoguanine 1:
2.4.2.29;

Protein crystallography data

The structure of Trna Guanine Transglycosylase (Tgt) in Complex with Furanoside-Based Lin-Benzoguanine 1, PDB code: 4leq was solved by F.R.Ehrmann, A.Heine, G.Klebe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.88 / 1.41
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 90.623, 65.106, 70.357, 90.00, 96.30, 90.00
R / Rfree (%) 12.3 / 14.8

Other elements in 4leq:

The structure of Trna Guanine Transglycosylase (Tgt) in Complex with Furanoside-Based Lin-Benzoguanine 1 also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Trna Guanine Transglycosylase (Tgt) in Complex with Furanoside-Based Lin-Benzoguanine 1 (pdb code 4leq). 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 Trna Guanine Transglycosylase (Tgt) in Complex with Furanoside-Based Lin-Benzoguanine 1, PDB code: 4leq:

Chlorine binding site 1 out of 1 in 4leq

Go back to Chlorine Binding Sites List in 4leq
Chlorine binding site 1 out of 1 in the Trna Guanine Transglycosylase (Tgt) in Complex with Furanoside-Based Lin-Benzoguanine 1


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Trna Guanine Transglycosylase (Tgt) in Complex with Furanoside-Based Lin-Benzoguanine 1 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl405

b:17.1
occ:1.00
 O A:HOH614 2.7 23.9 1.0
OG1 A:THR285 3.0 11.9 1.0
O A:HOH523 3.1 12.8 1.0
NH1 A:ARG289 3.2 14.4 1.0
CB A:THR285 3.6 11.2 1.0
O A:HOH797 3.7 32.0 1.0
N A:ARG286 3.8 10.8 1.0
NH2 A:ARG289 3.8 15.3 1.0
CB A:VAL282 3.9 11.6 1.0
CZ A:ARG289 4.0 14.5 1.0
O A:HOH589 4.0 20.5 1.0
CB A:ARG286 4.0 12.8 1.0
CD A:LYS52 4.1 14.2 1.0
CA A:ARG286 4.2 11.1 1.0
CG1 A:VAL282 4.2 13.4 1.0
CE A:LYS52 4.2 17.2 1.0
O A:VAL282 4.3 11.8 1.0
C A:THR285 4.3 10.9 1.0
CG A:LYS52 4.4 11.8 1.0
CA A:THR285 4.5 10.9 1.0
CA A:VAL282 4.6 10.8 1.0
CG2 A:THR285 4.7 12.3 1.0
CB A:LYS52 4.7 10.4 1.0
C A:VAL282 4.9 10.6 1.0
O A:HOH530 4.9 12.2 1.0
O A:VAL45 5.0 11.7 1.0

Reference:

L.J.Barandun, F.R.Ehrmann, D.Zimmerli, F.Immekus, M.Giroud, C.Grunenfelder, W.B.Schweizer, B.Bernet, M.Betz, A.Heine, G.Klebe, F.Diederich. Replacement of Water Molecules in A Phosphate Binding Site By Furanoside-Appended Lin-Benzoguanine Ligands of Trna-Guanine Transglycosylase (Tgt). Chemistry 2014.
ISSN: ISSN 0947-6539
PubMed: 25483606
DOI: 10.1002/CHEM.201405764
Page generated: Sat Dec 12 10:52:40 2020

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