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Chlorine in PDB 5i9l: Crystal Structure of B. Pseudomallei Fabi in Complex with Nad and PT404

Enzymatic activity of Crystal Structure of B. Pseudomallei Fabi in Complex with Nad and PT404

All present enzymatic activity of Crystal Structure of B. Pseudomallei Fabi in Complex with Nad and PT404:
1.3.1.9;

Protein crystallography data

The structure of Crystal Structure of B. Pseudomallei Fabi in Complex with Nad and PT404, PDB code: 5i9l was solved by M.W.Hirschbeck, S.Eltschkner, P.J.Tonge, C.Kisker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.53 / 1.80
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.579, 75.063, 86.375, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 21.4

Other elements in 5i9l:

The structure of Crystal Structure of B. Pseudomallei Fabi in Complex with Nad and PT404 also contains other interesting chemical elements:

Fluorine (F) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of B. Pseudomallei Fabi in Complex with Nad and PT404 (pdb code 5i9l). 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 B. Pseudomallei Fabi in Complex with Nad and PT404, PDB code: 5i9l:

Chlorine binding site 1 out of 1 in 5i9l

Go back to Chlorine Binding Sites List in 5i9l
Chlorine binding site 1 out of 1 in the Crystal Structure of B. Pseudomallei Fabi in Complex with Nad and PT404


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 B. Pseudomallei Fabi in Complex with Nad and PT404 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl302

b:60.8
occ:1.00
 CL A:9W7302 0.0 60.8 1.0
C11 A:9W7302 1.7 41.4 1.0
C10 A:9W7302 2.7 40.5 1.0
C6 A:9W7302 2.7 36.0 1.0
O1 A:9W7302 2.9 36.7 1.0
C3D A:NAD301 3.4 31.5 1.0
O A:GLY93 3.4 33.8 1.0
C2D A:NAD301 3.5 26.9 1.0
O2D A:NAD301 3.6 32.9 1.0
CA A:GLY93 3.6 31.6 1.0
O5D A:NAD301 3.7 38.5 1.0
CB A:ALA196 3.7 48.0 1.0
C A:GLY93 3.7 32.0 1.0
N A:GLY93 3.7 29.8 1.0
C9 A:9W7302 4.0 46.5 1.0
C7 A:9W7302 4.0 46.0 1.0
C5B A:NAD301 4.0 43.2 1.0
O3D A:NAD301 4.2 29.7 1.0
C5 A:9W7302 4.3 40.4 1.0
C5D A:NAD301 4.4 38.6 1.0
C8 A:9W7302 4.5 44.7 1.0
O3 A:NAD301 4.5 46.0 1.0
CE A:MET159 4.5 49.3 1.0
C4D A:NAD301 4.5 32.6 1.0
O4B A:NAD301 4.5 41.5 1.0
C A:ILE92 4.6 29.4 1.0
O A:HOH443 4.7 48.4 1.0
PN A:NAD301 4.7 40.0 1.0
N A:PHE94 4.8 34.0 1.0
O5B A:NAD301 4.9 45.5 1.0
C4B A:NAD301 4.9 43.8 1.0
C1D A:NAD301 4.9 27.7 1.0
O A:9W7302 4.9 31.2 1.0

Reference:

C.Neckles, S.Eltschkner, J.E.Cummings, M.Hirschbeck, F.Daryaee, G.R.Bommineni, Z.Zhang, L.Spagnuolo, W.Yu, S.Davoodi, R.A.Slayden, C.Kisker, P.J.Tonge. Rationalizing the Binding Kinetics For the Inhibition of the Burkholderia Pseudomallei FABI1 Enoyl-Acp Reductase. Biochemistry V. 56 1865 2017.
ISSN: ISSN 1520-4995
PubMed: 28225601
DOI: 10.1021/ACS.BIOCHEM.6B01048
Page generated: Sat Jul 12 03:02:21 2025

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