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Chlorine in PDB 3u0e: Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis in Complex with Fragment 9320

Enzymatic activity of Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis in Complex with Fragment 9320

All present enzymatic activity of Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis in Complex with Fragment 9320:
2.3.1.41;

Protein crystallography data

The structure of Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis in Complex with Fragment 9320, PDB code: 3u0e was solved by Seattle Structural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.60
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 78.070, 83.750, 73.610, 90.00, 121.50, 90.00
R / Rfree (%) 13.7 / 15.6

Other elements in 3u0e:

The structure of Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis in Complex with Fragment 9320 also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis in Complex with Fragment 9320 (pdb code 3u0e). 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 Beta-Ketoacyl Synthase From Brucella Melitensis in Complex with Fragment 9320, PDB code: 3u0e:

Chlorine binding site 1 out of 1 in 3u0e

Go back to Chlorine Binding Sites List in 3u0e
Chlorine binding site 1 out of 1 in the Crystal Structure of Beta-Ketoacyl Synthase From Brucella Melitensis in Complex with Fragment 9320


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 Beta-Ketoacyl Synthase From Brucella Melitensis in Complex with Fragment 9320 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:30.8
occ:1.00
 N A:MET267 3.4 11.7 1.0
OD1 A:ASP266 3.6 21.4 1.0
O A:HOH810 3.7 35.1 1.0
CB A:MET267 3.8 11.7 1.0
CA A:ASP266 4.1 12.9 1.0
CG A:ASP266 4.2 16.2 1.0
C A:ASP266 4.2 12.1 1.0
CA A:MET267 4.3 11.7 1.0
O A:TYR265 4.5 12.6 1.0
CB A:ASP266 4.7 14.7 1.0
OD2 A:ASP266 4.8 17.1 1.0
O A:HOH815 5.0 41.1 1.0

Reference:

E.I.Patterson, J.D.Nanson, J.Abendroth, C.Bryan, B.Sankaran, P.J.Myler, J.K.Forwood. Structural Characterization of Beta-Ketoacyl Acp Synthase I Bound to Platencin and Fragment Screening Molecules at Two Substrate Binding Sites. Proteins 2019.
ISSN: ESSN 1097-0134
PubMed: 31237717
DOI: 10.1002/PROT.25765
Page generated: Sun Jul 21 05:45:19 2024

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